167 results on '"Kloos, Marco"'
Search Results
2. SARS-CoV-2 Mpro responds to oxidation by forming disulfide and NOS/SONOS bonds
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Reinke, Patrick Y. A., Schubert, Robin, Oberthür, Dominik, Galchenkova, Marina, Rahmani Mashhour, Aida, Günther, Sebastian, Chretien, Anaïs, Round, Adam, Seychell, Brandon Charles, Norton-Baker, Brenna, Kim, Chan, Schmidt, Christina, Koua, Faisal H. M., Tolstikova, Alexandra, Ewert, Wiebke, Peña Murillo, Gisel Esperanza, Mills, Grant, Kirkwood, Henry, Brognaro, Hévila, Han, Huijong, Koliyadu, Jayanath, Schulz, Joachim, Bielecki, Johan, Lieske, Julia, Maracke, Julia, Knoska, Juraj, Lorenzen, Kristina, Brings, Lea, Sikorski, Marcin, Kloos, Marco, Vakili, Mohammad, Vagovic, Patrik, Middendorf, Philipp, de Wijn, Raphael, Bean, Richard, Letrun, Romain, Han, Seonghyun, Falke, Sven, Geng, Tian, Sato, Tokushi, Srinivasan, Vasundara, Kim, Yoonhee, Yefanov, Oleksandr M., Gelisio, Luca, Beck, Tobias, Doré, Andrew S., Mancuso, Adrian P., Betzel, Christian, Bajt, Saša, Redecke, Lars, Chapman, Henry N., Meents, Alke, Turk, Dušan, Hinrichs, Winfried, and Lane, Thomas J.
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- 2024
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3. 3D-Printed Sheet Jet for Stable Megahertz Liquid Sample Delivery at X-ray Free Electron Lasers
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Konold, Patrick E., You, Tong, Bielecki, Johan, Valerio, Joana, Kloos, Marco, Westphal, Daniel, Bellisario, Alfredo, Varma, Tej, Wolter, August, Koliyadu, Jayanath C. P., Koua, Faisal H. M., Letrun, Romain, Round, Adam, Sato, Tokushi, Mésźaros, Petra, Monrroy, Leonardo, Mutisya, Jennifer, Bódizs, Szabolcs, Larkiala, Taru, Nimmrich, Amke, Alvarez, Roberto, Bean, Richard, Ekeberg, Tomas, Kirian, Richard A., Westenhoff, Sebastian, and Maia, Filipe R. N. C.
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Physics - Instrumentation and Detectors ,Physics - Applied Physics ,Physics - Biological Physics - Abstract
X-ray Free Electron Lasers (XFELs) can probe chemical and biological reactions as they unfold with unprecedented spatial and temporal resolution. A principal challenge in this pursuit is the delivery of samples to the X-ray interaction point in a way that produces data of the highest possible quality and efficiency. This is hampered by constraints posed by the light source and operation within a beamline environment. For liquid samples, the solution typically involves a high-speed liquid jet, capable of keeping up with the rate of X-ray pulses. However, conventional jets are not ideal because of radiation-induced explosions of the jet, as well as their cylindrical geometry combined with the X-ray pointing instability of many beamlines causes the interaction volume to differ for every pulse. This complicates data analysis and contributes to measurement errors. An alternative geometry is a liquid sheet jet which, with its constant thickness over large areas, eliminates the X-ray pointing related problems. Since liquid sheets can be made very thin, the radiation-induced explosion is reduced, boosting their stability. They are especially attractive for experiments which benefit from small interaction volumes such as fluctuation X-ray scattering and several types of spectroscopy. Although they have seen increasing use for soft X-ray applications in recent years, there has not yet been wide-scale adoption at XFELs. Here, we demonstrate liquid sheet jet sample injection at the European XFEL. We evaluate several aspects of its performance relative to a conventional liquid jet including thickness profile, stability, and radiation-induced explosion dynamics at high repetition rates. The sheet jet exhibits superior performance across these critical experimental parameters. Its minute thickness also suggests ultrafast single-particle solution scattering is a possibility.
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- 2023
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4. New insights into the function and molecular mechanisms of Ferredoxin-NADP+ reductase from Brucella ovis
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Moreno, Andrea, Quereda-Moraleda, Isabel, Lozano-Vallhonrat, Celia, Buñuel-Escudero, María, Botha, Sabine, Kupitz, Christopher, Lisova, Stella, Sierra, Ray, Mariani, Valerio, Schleissner, Pamela, Gee, Leland B., Dörner, Katerina, Schmidt, Christina, Han, Huijong, Kloos, Marco, Smyth, Peter, Valerio, Joana, Schulz, Joachim, de Wijn, Raphael, Melo, Diogo V.M., Round, Adam, Trost, Fabian, Sobolev, Egor, Juncheng, E., Sikorski, Marcin, Bean, Richard, Martínez-Júlvez, Marta, Martin-Garcia, Jose Manuel, and Medina, Milagros
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- 2024
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5. Influence of pump laser fluence on ultrafast myoglobin structural dynamics
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Barends, Thomas R. M., Gorel, Alexander, Bhattacharyya, Swarnendu, Schirò, Giorgio, Bacellar, Camila, Cirelli, Claudio, Colletier, Jacques-Philippe, Foucar, Lutz, Grünbein, Marie Luise, Hartmann, Elisabeth, Hilpert, Mario, Holton, James M., Johnson, Philip J. M., Kloos, Marco, Knopp, Gregor, Marekha, Bogdan, Nass, Karol, Nass Kovacs, Gabriela, Ozerov, Dmitry, Stricker, Miriam, Weik, Martin, Doak, R. Bruce, Shoeman, Robert L., Milne, Christopher J., Huix-Rotllant, Miquel, Cammarata, Marco, and Schlichting, Ilme
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- 2024
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6. Rational Control of Off‐State Heterogeneity in a Photoswitchable Fluorescent Protein Provides Switching Contrast Enhancement**
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Adam, Virgile, Hadjidemetriou, Kyprianos, Jensen, Nickels, Shoeman, Robert L, Woodhouse, Joyce, Aquila, Andrew, Banneville, Anne‐Sophie, Barends, Thomas RM, Bezchastnov, Victor, Boutet, Sébastien, Byrdin, Martin, Cammarata, Marco, Carbajo, Sergio, Christou, Nina Eleni, Coquelle, Nicolas, De la Mora, Eugenio, Khatib, Mariam El, Chicano, Tadeo Moreno, Doak, R Bruce, Fieschi, Franck, Foucar, Lutz, Glushonkov, Oleksandr, Gorel, Alexander, Grünbein, Marie Luise, Hilpert, Mario, Hunter, Mark, Kloos, Marco, Koglin, Jason E, Lane, Thomas J, Liang, Mengning, Mantovanelli, Angela, Nass, Karol, Kovacs, Gabriela Nass, Owada, Shigeki, Roome, Christopher M, Schirò, Giorgio, Seaberg, Matthew, Stricker, Miriam, Thépaut, Michel, Tono, Kensuke, Ueda, Kiyoshi, Uriarte, Lucas M, You, Daehyun, Zala, Ninon, Domratcheva, Tatiana, Jakobs, Stefan, Sliwa, Michel, Schlichting, Ilme, Colletier, Jacques‐Philippe, Bourgeois, Dominique, and Weik, Martin
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Macromolecular and Materials Chemistry ,Chemical Sciences ,Physical Chemistry ,Escherichia coli ,Green Fluorescent Proteins ,Luminescent Proteins ,Microscopy ,nanoscopy ,photoswitchable fluorescent proteins ,serial femtosecond crystallography ,switching contrast ,quantum chemistry ,Atomic ,Molecular ,Nuclear ,Particle and Plasma Physics ,Physical Chemistry (incl. Structural) ,Theoretical and Computational Chemistry ,Chemical Physics ,Macromolecular and materials chemistry ,Physical chemistry - Abstract
Reversibly photoswitchable fluorescent proteins are essential markers for advanced biological imaging, and optimization of their photophysical properties underlies improved performance and novel applications. Here we establish a link between photoswitching contrast, one of the key parameters that dictate the achievable resolution in nanoscopy applications, and chromophore conformation in the non-fluorescent state of rsEGFP2, a widely employed label in REversible Saturable OpticaL Fluorescence Transitions (RESOLFT) microscopy. Upon illumination, the cis chromophore of rsEGFP2 isomerizes to two distinct off-state conformations, trans1 and trans2, located on either side of the V151 side chain. Reducing or enlarging the side chain at this position (V151A and V151L variants) leads to single off-state conformations that exhibit higher and lower switching contrast, respectively, compared to the rsEGFP2 parent. The combination of structural information obtained by serial femtosecond crystallography with high-level quantum chemical calculations and with spectroscopic and photophysical data determined in vitro suggests that the changes in switching contrast arise from blue- and red-shifts of the absorption bands associated to trans1 and trans2, respectively. Thus, due to elimination of trans2, the V151A variants of rsEGFP2 and its superfolding variant rsFolder2 display a more than two-fold higher switching contrast than their respective parent proteins, both in vitro and in E. coli cells. The application of the rsFolder2-V151A variant is demonstrated in RESOLFT nanoscopy. Our study rationalizes the connection between structural and photophysical chromophore properties and suggests a means to rationally improve fluorescent proteins for nanoscopy applications.
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- 2022
7. Co-flow injection for serial crystallography at X-ray free-electron lasers.
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Doppler, Diandra, Rabbani, Mohammad, Letrun, Romain, Cruz Villarreal, Jorvani, Kim, Dai, Gandhi, Sahir, Egatz-Gomez, Ana, Sonker, Mukul, Chen, Joe, Koua, Faisal, Yang, Jayhow, Youssef, Mohamed, Mazalova, Victoria, Bajt, Saša, Shelby, Megan, Coleman, Matt, Wiedorn, Max, Knoska, Juraj, Schön, Silvan, Sato, Tokushi, Hunter, Mark, Hosseinizadeh, Ahmad, Kuptiz, Christopher, Nazari, Reza, Alvarez, Roberto, Karpos, Konstantinos, Zaare, Sahba, Dobson, Zachary, Discianno, Erin, Zhang, Shangji, Zook, James, Bielecki, Johan, de Wijn, Raphael, Round, Adam, Vagovic, Patrik, Kloos, Marco, Vakili, Mohammad, Ketawala, Gihan, Stander, Natasha, Olson, Tien, Morin, Katherine, Mondal, Jyotirmory, Nguyen, Jonathan, Meza-Aguilar, José, Kodis, Gerdenis, Vaiana, Sara, Martin-Garcia, Jose, Mariani, Valerio, Schwander, Peter, Schmidt, Marius, Messerschmidt, Marc, Ourmazd, Abbas, Zatsepin, Nadia, Weierstall, Uwe, Bruce, Barry, Mancuso, Adrian, Grant, Thomas, Barty, Anton, Chapman, Henry, Fromme, Raimund, Spence, John, Botha, Sabine, Fromme, Petra, Kirian, Richard, Ros, Alexandra, and Frank, Matthias
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3D printing ,X-ray free-electron lasers ,XFELs ,microfluidic devices ,sample consumption ,serial crystallography ,viscous media - Abstract
Serial femtosecond crystallography (SFX) is a powerful technique that exploits X-ray free-electron lasers to determine the structure of macro-molecules at room temperature. Despite the impressive exposition of structural details with this novel crystallographic approach, the methods currently available to introduce crystals into the path of the X-ray beam sometimes exhibit serious drawbacks. Samples requiring liquid injection of crystal slurries consume large quantities of crystals (at times up to a gram of protein per data set), may not be compatible with vacuum configurations on beamlines or provide a high background due to additional sheathing liquids present during the injection. Proposed and characterized here is the use of an immiscible inert oil phase to supplement the flow of sample in a hybrid microfluidic 3D-printed co-flow device. Co-flow generation is reported with sample and oil phases flowing in parallel, resulting in stable injection conditions for two different resin materials experimentally. A numerical model is presented that adequately predicts these flow-rate conditions. The co-flow generating devices reduce crystal clogging effects, have the potential to conserve protein crystal samples up to 95% and will allow degradation-free light-induced time-resolved SFX.
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- 2022
8. De novo determination of mosquitocidal Cry11Aa and Cry11Ba structures from naturally-occurring nanocrystals
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Tetreau, Guillaume, Sawaya, Michael R, De Zitter, Elke, Andreeva, Elena A, Banneville, Anne-Sophie, Schibrowsky, Natalie A, Coquelle, Nicolas, Brewster, Aaron S, Grünbein, Marie Luise, Kovacs, Gabriela Nass, Hunter, Mark S, Kloos, Marco, Sierra, Raymond G, Schiro, Giorgio, Qiao, Pei, Stricker, Myriam, Bideshi, Dennis, Young, Iris D, Zala, Ninon, Engilberge, Sylvain, Gorel, Alexander, Signor, Luca, Teulon, Jean-Marie, Hilpert, Mario, Foucar, Lutz, Bielecki, Johan, Bean, Richard, de Wijn, Raphael, Sato, Tokushi, Kirkwood, Henry, Letrun, Romain, Batyuk, Alexander, Snigireva, Irina, Fenel, Daphna, Schubert, Robin, Canfield, Ethan J, Alba, Mario M, Laporte, Frédéric, Després, Laurence, Bacia, Maria, Roux, Amandine, Chapelle, Christian, Riobé, François, Maury, Olivier, Ling, Wai Li, Boutet, Sébastien, Mancuso, Adrian, Gutsche, Irina, Girard, Eric, Barends, Thomas RM, Pellequer, Jean-Luc, Park, Hyun-Woo, Laganowsky, Arthur D, Rodriguez, Jose, Burghammer, Manfred, Shoeman, Robert L, Doak, R Bruce, Weik, Martin, Sauter, Nicholas K, Federici, Brian, Cascio, Duilio, Schlichting, Ilme, and Colletier, Jacques-Philippe
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Inorganic Chemistry ,Biochemistry and Cell Biology ,Chemical Sciences ,Biological Sciences ,Animals ,Bacillus thuringiensis ,Bacterial Proteins ,Endotoxins ,Hemolysin Proteins ,Larva ,Mosquito Control ,Nanoparticles - Abstract
Cry11Aa and Cry11Ba are the two most potent toxins produced by mosquitocidal Bacillus thuringiensis subsp. israelensis and jegathesan, respectively. The toxins naturally crystallize within the host; however, the crystals are too small for structure determination at synchrotron sources. Therefore, we applied serial femtosecond crystallography at X-ray free electron lasers to in vivo-grown nanocrystals of these toxins. The structure of Cry11Aa was determined de novo using the single-wavelength anomalous dispersion method, which in turn enabled the determination of the Cry11Ba structure by molecular replacement. The two structures reveal a new pattern for in vivo crystallization of Cry toxins, whereby each of their three domains packs with a symmetrically identical domain, and a cleavable crystal packing motif is located within the protoxin rather than at the termini. The diversity of in vivo crystallization patterns suggests explanations for their varied levels of toxicity and rational approaches to improve these toxins for mosquito control.
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- 2022
9. Form factor determination of biological molecules with X-ray free electron laser small-angle scattering (XFEL-SAS)
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Blanchet, Clement E., Round, Adam, Mertens, Haydyn D. T., Ayyer, Kartik, Graewert, Melissa, Awel, Salah, Franke, Daniel, Dörner, Katerina, Bajt, Saša, Bean, Richard, Custódio, Tânia F., de Wijn, Raphael, Juncheng, E., Henkel, Alessandra, Gruzinov, Andrey, Jeffries, Cy M., Kim, Yoonhee, Kirkwood, Henry, Kloos, Marco, Knoška, Juraj, Koliyadu, Jayanath, Letrun, Romain, Löw, Christian, Makroczyova, Jana, Mall, Abhishek, Meijers, Rob, Pena Murillo, Gisel Esperanza, Oberthür, Dominik, Round, Ekaterina, Seuring, Carolin, Sikorski, Marcin, Vagovic, Patrik, Valerio, Joana, Wollweber, Tamme, Zhuang, Yulong, Schulz, Joachim, Haas, Heinrich, Chapman, Henry N., Mancuso, Adrian P., and Svergun, Dmitri
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- 2023
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10. Observation of substrate diffusion and ligand binding in enzyme crystals using high-repetition-rate mix-and-inject serial crystallography
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Pandey, Suraj, Calvey, George, Katz, Andrea M, Malla, Tek Narsingh, Koua, Faisal HM, Martin-Garcia, Jose M, Poudyal, Ishwor, Yang, Jay-How, Vakili, Mohammad, Yefanov, Oleksandr, Zielinski, Kara A, Bajt, Sasa, Awel, Salah, Doerner, Katarina, Frank, Matthias, Gelisio, Luca, Jernigan, Rebecca, Kirkwood, Henry, Kloos, Marco, Koliyadu, Jayanath, Mariani, Valerio, Miller, Mitchell D, Mills, Grant, Nelson, Garrett, Olmos, Jose L, Sadri, Alireza, Sato, Tokushi, Tolstikova, Alexandra, Xu, Weijun, Ourmazd, Abbas, Spence, John CH, Schwander, Peter, Barty, Anton, Chapman, Henry N, Fromme, Petra, Mancuso, Adrian P, Phillips, George N, Bean, Richard, Pollack, Lois, and Schmidt, Marius
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Tuberculosis ,Rare Diseases ,Good Health and Well Being ,substrate diffusion in crystals ,antibiotic resistance ,beta-lactamases ,enzyme kinetics ,irreversible inhibition ,mix-and-inject serial crystallography ,serial femtosecond crystallography ,European X-ray Free-Electron Laser ,megahertz pulse-repetition rate ,protein structure determination ,drug discovery ,ceftriaxone ,sulbactam ,X-ray crystallography ,enzyme mechanisms ,β-lactamases ,Atomic ,Molecular ,Nuclear ,Particle and Plasma Physics ,Condensed Matter Physics ,Physical Chemistry (incl. Structural) - Abstract
Here, we illustrate what happens inside the catalytic cleft of an enzyme when substrate or ligand binds on single-millisecond timescales. The initial phase of the enzymatic cycle is observed with near-atomic resolution using the most advanced X-ray source currently available: the European XFEL (EuXFEL). The high repetition rate of the EuXFEL combined with our mix-and-inject technology enables the initial phase of ceftriaxone binding to the Mycobacterium tuberculosis β-lactamase to be followed using time-resolved crystallography in real time. It is shown how a diffusion coefficient in enzyme crystals can be derived directly from the X-ray data, enabling the determination of ligand and enzyme-ligand concentrations at any position in the crystal volume as a function of time. In addition, the structure of the irreversible inhibitor sulbactam bound to the enzyme at a 66 ms time delay after mixing is described. This demonstrates that the EuXFEL can be used as an important tool for biomedically relevant research.
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- 2021
11. De novo determination of mosquitocidal Cry11Aa and Cry11Ba structures from naturally-occurring nanocrystals
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Tetreau, Guillaume, Sawaya, Michael R, De Zitter, Elke, Andreeva, Elena A, Banneville, Anne-Sophie, Schibrowsky, Natalie, Coquelle, Nicolas, Brewster, Aaron S, Grünbein, Marie Luise, Kovacs, Gabriela Nass, Hunter, Mark S, Kloos, Marco, Sierra, Raymond G, Schiro, Giorgio, Qiao, Pei, Stricker, Myriam, Bideshi, Dennis, Young, Iris D, Zala, Ninon, Engilberge, Sylvain, Gorel, Alexander, Signor, Luca, Teulon, Jean-Marie, Hilpert, Mario, Foucar, Lutz, Bielecki, Johan, Bean, Richard, de Wijn, Raphael, Sato, Tokushi, Kirkwood, Henry, Letrun, Romain, Batyuk, Alexander, Snigireva, Irina, Fenel, Daphna, Schubert, Robin, Canfield, Ethan J, Alba, Mario M, Laporte, Frédéric, Després, Laurence, Bacia, Maria, Roux, Amandine, Chapelle, Christian, Riobé, François, Maury, Olivier, Ling, Wai Li, Boutet, Sébastien, Mancuso, Adrian, Gutsche, Irina, Girard, Eric, Barends, Thomas RM, Pellequer, Jean-Luc, Park, Hyun-Woo, Laganowsky, Arthur D, Rodriguez, Jose, Burghammer, Manfred, Shoeman, Robert L, Doak, R Bruce, Weik, Martin, Sauter, Nicholas K, Federici, Brian, Cascio, Duilio, Schlichting, Ilme, and Colletier, Jacques-Philippe
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Inorganic Chemistry ,Biochemistry and Cell Biology ,Chemical Sciences ,Biological Sciences - Abstract
Cry11Aa and Cry11Ba are the two most potent toxins produced by mosquitocidal Bacillus thuringiensis subsp. israelensis and jegathesan , respectively. The toxins naturally crystallize within the host; however, the crystals are too small for structure determination at synchrotron sources. Therefore, we applied serial femtosecond crystallography at X-ray free electron lasers to in vivo -grown nanocrystals of these toxins. The structure of Cry11Aa was determined de novo using the single-wavelength anomalous dispersion method, which in turn enabled the determination of the Cry11Ba structure by molecular replacement. The two structures reveal a new pattern for in vivo crystallization of Cry toxins, whereby each of their three domains packs with a symmetrically identical domain, and a cleavable crystal packing motif is located within the protoxin rather than at the termini. The diversity of in vivo crystallization patterns suggests explanations for their varied levels of toxicity and rational approaches to improve these toxins for mosquito control.
- Published
- 2021
12. Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin
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Kovacs, Gabriela Nass, Colletier, Jacques-Philippe, Grünbein, Marie, Yang, Yang, Stensitzki, Till, Batyuk, Alexander, Carbajo, Sergio, Doak, R, Ehrenberg, David, Foucar, Lutz, Gasper, Raphael, Gorel, Alexander, Hilpert, Mario, Kloos, Marco, Koglin, Jason, Reinstein, Jochen, Roome, Christopher, Schlesinger, Ramona, Seaberg, Matthew, Shoeman, Robert, Stricker, Miriam, Boutet, Sébastien, Haacke, Stefan, Heberle, Joachim, Heyne, Karsten, Domratcheva, Tatiana, Barends, Thomas, and Schlichting, Ilme
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Physics - Biological Physics ,Quantitative Biology - Biomolecules - Abstract
Bacteriorhodopsin (bR) is a light-driven proton pump. We use time-resolved crystallography at an X-ray free-electron laser to follow the structural changes in multiphoton-excited bR from 250 femtoseconds to 10 picoseconds. Quantum chemistry and ultrafast spectroscopy allow identifying a sequential two-photon absorption process, leading to excitation of a tryptophan residue flanking the retinal chromophore, as a first manifestation of multi-photon effects. We resolve distinct stages in the structural dynamics of the all-trans retinal in photoexcited bR to a highly twisted 13-cis conformation. Other active site sub-picosecond rearrangements include correlated vibrational motions of the electronically excited retinal chromophore, the surrounding amino acids and water molecules as well as their hydrogen bonding network. These results show that this extended photo-active network forms an electronically and vibrationally coupled system in bR, and most likely in all retinal proteins.
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- 2019
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13. A multi-million image Serial Femtosecond Crystallography dataset collected at the European XFEL
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Kirkwood, Henry J., de Wijn, Raphael, Mills, Grant, Letrun, Romain, Kloos, Marco, Vakili, Mohammad, Karnevskiy, Mikhail, Ahmed, Karim, Bean, Richard J., Bielecki, Johan, Dall’Antonia, Fabio, Kim, Yoonhee, Kim, Chan, Koliyadu, Jayanath, Round, Adam, Sato, Tokushi, Sikorski, Marcin, Vagovič, Patrik, Sztuk-Dambietz, Jolanta, and Mancuso, Adrian P.
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- 2022
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14. Crystallographic Studies of Rhodopsins: Structure and Dynamics
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Grünbein, Marie Luise, primary, Kovacs, Gabriela Nass, additional, Kloos, Marco, additional, Gorel, Alexander, additional, Doak, R. Bruce, additional, Shoeman, Robert L., additional, Barends, Thomas R. M., additional, and Schlichting, Ilme, additional
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- 2022
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15. Crystal structure of a bacterial photoactivated adenylate cyclase determined at room temperature by serial femtosecond crystallography
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Kapetanaki, Sofia M, primary, Coquelle, Nicolas, additional, von Stetten, David, additional, Byrdin, Martin, additional, Rios-Santacruz, Ronald, additional, Bean, Richard, additional, Bielecki, Johan, additional, Boudjelida, Mohamed, additional, Fekete, Zsuzsana, additional, Grime, Geoffrey W, additional, Han, Huijong, additional, Hatton, Caitlin, additional, Kantamneni, Sravya, additional, Kharitonov, Konstantin, additional, Kim, Chan, additional, Kloos, Marco, additional, Koua, Faisal H.M., additional, de Diego Martinez, Inaki, additional, Melo, Diogo, additional, Rane, Lukas, additional, Round, Adam, additional, Round, Ekaterina, additional, Sarma, Abhisakh, additional, Schubert, Robin, additional, Schulz, Joachim, additional, Sikorski, Marcin, additional, Vakili, Mohammad, additional, Valerio, Joana, additional, Vitas, Jovana, additional, de Wijn, Raphael, additional, Wrona, Agnieszka, additional, Zala, Ninon, additional, Pearson, Arwen, additional, Dorner, Katerina, additional, Schiro, Giorgio, additional, Garman, Elspeth F, additional, Lukacs, Andras, additional, and Weik, Martin, additional
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- 2024
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16. Insights into an efficient light-driven hybrid P450 BM3 enzyme from crystallographic, spectroscopic and biochemical studies
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Spradlin, Jessica, Lee, Diana, Mahadevan, Sruthi, Mahomed, Mavish, Tang, Lawrence, Lam, Quan, Colbert, Alexander, Shafaat, Oliver S, Goodin, David, Kloos, Marco, Kato, Mallory, and Cheruzel, Lionel E
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Biochemistry and Cell Biology ,Biological Sciences ,Amino Acid Substitution ,Bacterial Proteins ,Crystallography ,X-Ray ,Cytochrome P-450 Enzyme System ,Electron Transport ,Heme ,Kinetics ,Models ,Molecular ,Mutagenesis ,Site-Directed ,NADPH-Ferrihemoprotein Reductase ,Photochemical Processes ,Protein Conformation ,Recombinant Fusion Proteins ,Spectrophotometry ,Cytochrome P450 ,Electron transfer ,Hybrid P450 BM3 enzymes ,Crystal structure ,Enzyme catalysis ,Photocatalytic activity ,Physical Sciences ,Biological sciences ,Physical sciences - Abstract
BackgroundIn order to perform selective CH functionalization upon visible light irradiation, Ru(II)-diimine functionalized P450 heme enzymes have been developed. The sL407C-1 enzyme containing the Ru(bpy)2PhenA (bpy=2,2'-bipyridine and PhenA=5-acetamido-1,10-phenanthroline) photosensitizer (1) covalently attached to the non-native single cysteine L407C of the P450BM3 heme domain mutant, displays high photocatalytic activity in the selective CH bond hydroxylation of several substrates.MethodsA combination of X-ray crystallography, site-directed mutagenesis, transient absorption measurements and enzymatic assays was used to gain insights into its photocatalytic activity and electron transfer pathway.ResultsThe crystal structure of the sL407C-1 enzyme was solved in the open and closed conformations revealing a through-space electron transfer pathway involving highly conserved, F393 and Q403, residues. Several mutations of these residues (F393A, F393W or Q403W) were introduced to probe their roles in the overall reaction. Transient absorption measurements confirm rapid electron transfer as heme reduction is observed in all four hybrid enzymes. Compared to the parent sL407C-1, photocatalytic activity was negligible in the dF393A-1 enzyme while 60% increase in activity with total turnover numbers of 420 and 90% product conversion was observed with the dQ403W-1 mutant.ConclusionsIn the sL407C-1 enzyme, the photosensitizer is ideally located to rapidly deliver electrons, using the naturally occurring electron transfer pathway, to the heme center in order to activate molecular dioxygen and sustain photocatalytic activity.General significanceThe results shed light on the design of efficient light-driven biocatalysts and the approach can be generalized to other members of the P450 superfamily.
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- 2016
17. Illumination guidelines for ultrafast pump–probe experiments by serial femtosecond crystallography
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Grünbein, Marie Luise, Stricker, Miriam, Nass Kovacs, Gabriela, Kloos, Marco, Doak, R. Bruce, Shoeman, Robert L., Reinstein, Jochen, Lecler, Sylvain, Haacke, Stefan, and Schlichting, Ilme
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- 2020
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18. Effect of X-ray free-electron laser-induced shockwaves on haemoglobin microcrystals delivered in a liquid jet
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Grünbein, Marie Luise, Gorel, Alexander, Foucar, Lutz, Carbajo, Sergio, Colocho, William, Gilevich, Sasha, Hartmann, Elisabeth, Hilpert, Mario, Hunter, Mark, Kloos, Marco, Koglin, Jason E., Lane, Thomas J., Lewandowski, Jim, Lutman, Alberto, Nass, Karol, Nass Kovacs, Gabriela, Roome, Christopher M., Sheppard, John, Shoeman, Robert L., Stricker, Miriam, van Driel, Tim, Vetter, Sharon, Doak, R. Bruce, Boutet, Sébastien, Aquila, Andrew, Decker, Franz Josef, Barends, Thomas R. M., Stan, Claudiu Andrei, and Schlichting, Ilme
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- 2021
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19. Microsecond time-resolved X-ray scattering by utilizing MHz repetition rate at second-generation XFELs
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Westenhoff, Sebastian, primary, Konold, Patrick, additional, Monrroy, Leonardo, additional, Bellisario, Alfredo, additional, Filipe, Diogo, additional, Adams, Patrick, additional, Alvarez, Roberto, additional, Bean, Richard, additional, Bielecki, Johan, additional, Bódizs, Szabolcs, additional, Ducroq, Gabriel, additional, Grubmueller, Helmut, additional, Kirian, Richard, additional, Kloos, Marco, additional, Koliyadu, Jayanat, additional, Koua, Faisal, additional, Larkiala, Taru, additional, Letrun, Romain, additional, Lindsten, Fredrik, additional, Maihöfer, Michael, additional, Martin, Andrew, additional, Mészáros, Petra, additional, Mutisya, Jennifer, additional, Nimmrich, Amke, additional, Okamoto, Kenta, additional, Round, Adam, additional, Sato, Tokushi, additional, Valerio, Joana, additional, Westphal, Daniel, additional, Wolter, August, additional, Yenupuri, Tej, additional, You, Tong, additional, and Maia, Filipe, additional
- Published
- 2023
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20. Structure of the Lysinibacillus sphaericus Tpp49Aa1 pesticidal protein elucidated from natural crystals using MHz-SFX
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Williamson, Lainey J., primary, Galchenkova, Marina, additional, Best, Hannah L., additional, Bean, Richard J., additional, Munke, Anna, additional, Awel, Salah, additional, Pena, Gisel, additional, Knoska, Juraj, additional, Schubert, Robin, additional, Dörner, Katerina, additional, Park, Hyun-Woo, additional, Bideshi, Dennis K., additional, Henkel, Alessandra, additional, Kremling, Viviane, additional, Klopprogge, Bjarne, additional, Lloyd-Evans, Emyr, additional, Young, Mark T., additional, Valerio, Joana, additional, Kloos, Marco, additional, Sikorski, Marcin, additional, Mills, Grant, additional, Bielecki, Johan, additional, Kirkwood, Henry, additional, Kim, Chan, additional, de Wijn, Raphael, additional, Lorenzen, Kristina, additional, Xavier, Paul Lourdu, additional, Rahmani Mashhour, Aida, additional, Gelisio, Luca, additional, Yefanov, Oleksandr, additional, Mancuso, Adrian P., additional, Federici, Brian A., additional, Chapman, Henry N., additional, Crickmore, Neil, additional, Rizkallah, Pierre J., additional, Berry, Colin, additional, and Oberthür, Dominik, additional
- Published
- 2023
- Full Text
- View/download PDF
21. 3D-printed sheet jet for stable megahertz liquid sample delivery at X-ray free-electron lasers
- Author
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Konold, Patrick E., primary, You, Tong, additional, Bielecki, Johan, additional, Valerio, Joana, additional, Kloos, Marco, additional, Westphal, Daniel, additional, Bellisario, Alfredo, additional, Varma Yenupuri, Tej, additional, Wollter, August, additional, Koliyadu, Jayanath C. P., additional, Koua, Faisal H.M., additional, Letrun, Romain, additional, Round, Adam, additional, Sato, Tokushi, additional, Mészáros, Petra, additional, Monrroy, Leonardo, additional, Mutisya, Jennifer, additional, Bódizs, Szabolcs, additional, Larkiala, Taru, additional, Nimmrich, Amke, additional, Alvarez, Roberto, additional, Adams, Patrick, additional, Bean, Richard, additional, Ekeberg, Tomas, additional, Kirian, Richard A., additional, Martin, Andrew V., additional, Westenhoff, Sebastian, additional, and Maia, Filipe R. N. C., additional
- Published
- 2023
- Full Text
- View/download PDF
22. Structural dynamics in proteins induced by and probed with X-ray free-electron laser pulses
- Author
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Nass, Karol, Gorel, Alexander, Abdullah, Malik M., V. Martin, Andrew, Kloos, Marco, Marinelli, Agostino, Aquila, Andrew, Barends, Thomas R. M., Decker, Franz-Josef, Bruce Doak, R., Foucar, Lutz, Hartmann, Elisabeth, Hilpert, Mario, Hunter, Mark S., Jurek, Zoltan, Koglin, Jason E., Kozlov, Alexander, Lutman, Alberto A., Kovacs, Gabriela Nass, Roome, Christopher M., Shoeman, Robert L., Santra, Robin, Quiney, Harry M., Ziaja, Beata, Boutet, Sébastien, and Schlichting, Ilme
- Published
- 2020
- Full Text
- View/download PDF
23. Analysis of liquid-jet sample delivery stability at the European X-ray Free-Electron Laser using machine vision and image processing
- Author
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Patel, Jaydeep, primary, Round, Adam, additional, de Wijn, Raphaël, additional, Vakili, Mohammad, additional, Kloos, Marco, additional, Peele, Andrew, additional, Mancuso, Adrian, additional, and Abbey, Brian, additional
- Published
- 2023
- Full Text
- View/download PDF
24. XFEL Microcrystallography of Self-Assembling Silver n-Alkanethiolates
- Author
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Aleksich, Mariya, primary, Paley, Daniel W., additional, Schriber, Elyse A., additional, Linthicum, Will, additional, Oklejas, Vanessa, additional, Mittan-Moreau, David W., additional, Kelly, Ryan P., additional, Kotei, Patience A., additional, Ghodsi, Anita, additional, Sierra, Raymond G., additional, Aquila, Andrew, additional, Poitevin, Frédéric, additional, Blaschke, Johannes P., additional, Vakili, Mohammad, additional, Milne, Christopher J., additional, Dall’Antonia, Fabio, additional, Khakhulin, Dmitry, additional, Ardana-Lamas, Fernando, additional, Lima, Frederico, additional, Valerio, Joana, additional, Han, Huijong, additional, Gallo, Tamires, additional, Yousef, Hazem, additional, Turkot, Oleksii, additional, Bermudez Macias, Ivette J., additional, Kluyver, Thomas, additional, Schmidt, Philipp, additional, Gelisio, Luca, additional, Round, Adam R., additional, Jiang, Yifeng, additional, Vinci, Doriana, additional, Uemura, Yohei, additional, Kloos, Marco, additional, Hunter, Mark, additional, Mancuso, Adrian P., additional, Huey, Bryan D., additional, Parent, Lucas R., additional, Sauter, Nicholas K., additional, Brewster, Aaron S., additional, and Hohman, J. Nathan, additional
- Published
- 2023
- Full Text
- View/download PDF
25. Mix-and-extrude: high-viscosity sample injection towards time-resolved protein crystallography
- Author
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Vakili, Mohammad, primary, Han, Huijong, additional, Schmidt, Christina, additional, Wrona, Agnieszka, additional, Kloos, Marco, additional, de Diego, Iñaki, additional, Dörner, Katerina, additional, Geng, Tian, additional, Kim, Chan, additional, Koua, Faisal H. M., additional, Melo, Diogo V. M., additional, Rappas, Mathieu, additional, Round, Adam, additional, Round, Ekaterina, additional, Sikorski, Marcin, additional, Valerio, Joana, additional, Zhou, Tiankun, additional, Lorenzen, Kristina, additional, and Schulz, Joachim, additional
- Published
- 2023
- Full Text
- View/download PDF
26. MHz data collection of a microcrystalline mixture of different jack bean proteins
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Grünbein, Marie Luise, Bielecki, Johan, Gorel, Alexander, Stricker, Miriam, Bean, Richard, Cammarata, Marco, Dörner, Katerina, Fröhlich, Lars, Hartmann, Elisabeth, Hauf, Steffen, Hilpert, Mario, Kim, Yoonhee, Kloos, Marco, Letrun, Romain, Messerschmidt, Marc, Mills, Grant, Nass Kovacs, Gabriela, Ramilli, Marco, Roome, Christopher M., Sato, Tokushi, Scholz, Matthias, Sliwa, Michel, Sztuk-Dambietz, Jolanta, Weik, Martin, Weinhausen, Britta, Al-Qudami, Nasser, Boukhelef, Djelloul, Brockhauser, Sandor, Ehsan, Wajid, Emons, Moritz, Esenov, Sergey, Fangohr, Hans, Kaukher, Alexander, Kluyver, Thomas, Lederer, Max, Maia, Luis, Manetti, Maurizio, Michelat, Thomas, Münnich, Astrid, Pallas, Florent, Palmer, Guido, Previtali, Gianpietro, Raab, Natascha, Silenzi, Alessandro, Szuba, Janusz, Venkatesan, Sandhya, Wrona, Krzysztof, Zhu, Jun, Doak, R. Bruce, Shoeman, Robert L., Foucar, Lutz, Colletier, Jacques-Philippe, Mancuso, Adrian P., Barends, Thomas R. M., Stan, Claudiu A., and Schlichting, Ilme
- Published
- 2019
- Full Text
- View/download PDF
27. Megahertz data collection from protein microcrystals at an X-ray free-electron laser
- Author
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Grünbein, Marie Luise, Bielecki, Johan, Gorel, Alexander, Stricker, Miriam, Bean, Richard, Cammarata, Marco, Dörner, Katerina, Fröhlich, Lars, Hartmann, Elisabeth, Hauf, Steffen, Hilpert, Mario, Kim, Yoonhee, Kloos, Marco, Letrun, Romain, Messerschmidt, Marc, Mills, Grant, Nass Kovacs, Gabriela, Ramilli, Marco, Roome, Christopher M., Sato, Tokushi, Scholz, Matthias, Sliwa, Michel, Sztuk-Dambietz, Jolanta, Weik, Martin, Weinhausen, Britta, Al-Qudami, Nasser, Boukhelef, Djelloul, Brockhauser, Sandor, Ehsan, Wajid, Emons, Moritz, Esenov, Sergey, Fangohr, Hans, Kaukher, Alexander, Kluyver, Thomas, Lederer, Max, Maia, Luis, Manetti, Maurizio, Michelat, Thomas, Münnich, Astrid, Pallas, Florent, Palmer, Guido, Previtali, Gianpietro, Raab, Natascha, Silenzi, Alessandro, Szuba, Janusz, Venkatesan, Sandhya, Wrona, Krzysztof, Zhu, Jun, Doak, R. Bruce, Shoeman, Robert L., Foucar, Lutz, Colletier, Jacques-Philippe, Mancuso, Adrian P., Barends, Thomas R. M., Stan, Claudiu A., and Schlichting, Ilme
- Published
- 2018
- Full Text
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28. Mix-and-extrude using 3D printed nozzles for time-resolved membrane protein crystallography
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Vakili, Mohammad, primary, Han, Huijong, additional, Schmidt, Christina, additional, Wrona, Agnieszka, additional, Kloos, Marco, additional, de Diego, Iñaki, additional, Dörner, Katerina, additional, Valerio, Joana, additional, Round, Ekaterina, additional, Lorenzen, Kristina, additional, and Schulz, Joachim, additional
- Published
- 2022
- Full Text
- View/download PDF
29. Influence of pump laser fluence on ultrafast structural changes in myoglobin
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Barends, Thomas R.M., primary, Bhattacharyya, Swarnendu, additional, Gorel, Alexander, additional, Schiro, Giorgio, additional, Bacellar, Camila, additional, Cirelli, Claudio, additional, Colletier, Jacques-Philippe, additional, Foucar, Lutz, additional, Grünbein, Marie Luise, additional, Hartmann, Elisabeth, additional, Hilpert, Mario, additional, Johnson, Philip J.M., additional, Kloos, Marco, additional, Knopp, Gregor, additional, Marekha, Bogdan, additional, Nass, Karol, additional, Kovacs, Gabriela Nass, additional, Ozerov, Dmitry, additional, Stricker, Miriam, additional, Weik, Martin, additional, Doak, R. Bruce, additional, Shoeman, Robert L., additional, Milne, Christopher J., additional, Huix-Rotllant, Miquel, additional, Cammarata, Marco, additional, and Schlichting, Ilme, additional
- Published
- 2022
- Full Text
- View/download PDF
30. Cover Feature: Rational Control of Off‐State Heterogeneity in a Photoswitchable Fluorescent Protein Provides Switching Contrast Enhancement (ChemPhysChem 19/2022)
- Author
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Adam, Virgile, primary, Hadjidemetriou, Kyprianos, additional, Jensen, Nickels, additional, Shoeman, Robert L., additional, Woodhouse, Joyce, additional, Aquila, Andrew, additional, Banneville, Anne‐Sophie, additional, Barends, Thomas R. M., additional, Bezchastnov, Victor, additional, Boutet, Sébastien, additional, Byrdin, Martin, additional, Cammarata, Marco, additional, Carbajo, Sergio, additional, Eleni Christou, Nina, additional, Coquelle, Nicolas, additional, De la Mora, Eugenio, additional, El Khatib, Mariam, additional, Moreno Chicano, Tadeo, additional, Bruce Doak, R., additional, Fieschi, Franck, additional, Foucar, Lutz, additional, Glushonkov, Oleksandr, additional, Gorel, Alexander, additional, Grünbein, Marie Luise, additional, Hilpert, Mario, additional, Hunter, Mark, additional, Kloos, Marco, additional, Koglin, Jason E., additional, Lane, Thomas J., additional, Liang, Mengning, additional, Mantovanelli, Angela, additional, Nass, Karol, additional, Nass Kovacs, Gabriela, additional, Owada, Shigeki, additional, Roome, Christopher M., additional, Schirò, Giorgio, additional, Seaberg, Matthew, additional, Stricker, Miriam, additional, Thépaut, Michel, additional, Tono, Kensuke, additional, Ueda, Kiyoshi, additional, Uriarte, Lucas M., additional, You, Daehyun, additional, Zala, Ninon, additional, Domratcheva, Tatiana, additional, Jakobs, Stefan, additional, Sliwa, Michel, additional, Schlichting, Ilme, additional, Colletier, Jacques‐Philippe, additional, Bourgeois, Dominique, additional, and Weik, Martin, additional
- Published
- 2022
- Full Text
- View/download PDF
31. Functional Linkage of Adenine Nucleotide Binding Sites in Mammalian Muscle 6-Phosphofructokinase
- Author
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Brüser, Antje, Kirchberger, Jürgen, Kloos, Marco, Sträter, Norbert, and Schöneberg, Torsten
- Published
- 2012
- Full Text
- View/download PDF
32. 3D printed devices and infrastructure for liquid sample delivery at the European XFEL
- Author
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Vakili, Mohammad, primary, Bielecki, Johan, additional, Knoška, Juraj, additional, Otte, Florian, additional, Han, Huijong, additional, Kloos, Marco, additional, Schubert, Robin, additional, Delmas, Elisa, additional, Mills, Grant, additional, de Wijn, Raphael, additional, Letrun, Romain, additional, Dold, Simon, additional, Bean, Richard, additional, Round, Adam, additional, Kim, Yoonhee, additional, Lima, Frederico A., additional, Dörner, Katerina, additional, Valerio, Joana, additional, Heymann, Michael, additional, Mancuso, Adrian P., additional, and Schulz, Joachim, additional
- Published
- 2022
- Full Text
- View/download PDF
33. Structure of the Lysinibacillus sphaericus Tpp49Aa1 pesticidal protein elucidated from natural crystals using MHz-SFX
- Author
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Williamson, Lainey J, primary, Galchenkova, Marina, additional, Best, Hannah L, additional, Bean, Richard J, additional, Munke, Anna, additional, Awel, Salah, additional, Pena, Gisel, additional, Knoska, Juraj, additional, Schubert, Robin, additional, Doerner, Katerina, additional, Park, Hyun-Woo, additional, Bideshi, Dennis K, additional, Henkel, Alessandra, additional, Kremling, Viviane, additional, Klopprogge, Bjarne, additional, Lloyd-Evans, Emyr, additional, Young, Mark, additional, Valerio, Joana, additional, Kloos, Marco, additional, Sikorski, Marcin, additional, Mills, Grant, additional, Bielecki, Johan, additional, Kirkwood, Henry, additional, Kim, Chan, additional, de Wijn, Raphael, additional, Lorenzen, Kristina, additional, Xavier, P. Lourdu, additional, Rahmani, Aida, additional, Gelisio, Luca, additional, Yefanov, Oleksandr, additional, Mancuso, Adrian P, additional, Federici, Brian, additional, Chapman, Henry N, additional, Crickmore, Neil, additional, Rizkallah, Pierre J, additional, Berry, Colin, additional, and Oberthur, Dominik, additional
- Published
- 2022
- Full Text
- View/download PDF
34. De novo determination of mosquitocidal Cry11Aa and Cry11Ba structures from naturally-occurring nanocrystals
- Author
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Tetreau, Guillaume, primary, Sawaya, Michael R., additional, De Zitter, Elke, additional, Andreeva, Elena A., additional, Banneville, Anne-Sophie, additional, Schibrowsky, Natalie, additional, Coquelle, Nicolas, additional, Brewster, Aaron S., additional, Grünbein, Marie Luise, additional, Kovacs, Gabriela Nass, additional, Hunter, Mark S., additional, Kloos, Marco, additional, Sierra, Raymond G., additional, Schiro, Giorgio, additional, Qiao, Pei, additional, Stricker, Myriam, additional, Bideshi, Dennis, additional, Young, Iris D., additional, Zala, Ninon, additional, Engilberge, Sylvain, additional, Gorel, Alexander, additional, Signor, Luca, additional, Teulon, Jean-Marie, additional, Hilpert, Mario, additional, Foucar, Lutz, additional, Bielecki, Johan, additional, Bean, Richard, additional, de Wijn, Raphael, additional, Sato, Tokushi, additional, Kirkwood, Henry, additional, Letrun, Romain, additional, Batyuk, Alexander, additional, Snigireva, Irina, additional, Fenel, Daphna, additional, Schubert, Robin, additional, Canfield, Ethan J., additional, Alba, Mario M., additional, Laporte, Frédéric, additional, Després, Laurence, additional, Bacia, Maria, additional, Roux, Amandine, additional, Chapelle, Christian, additional, Riobé, François, additional, Maury, Olivier, additional, Ling, Wai Li, additional, Boutet, Sébastien, additional, Mancuso, Adrian, additional, Gutsche, Irina, additional, Girard, Eric, additional, Barends, Thomas R. M., additional, Pellequer, Jean-Luc, additional, Park, Hyun-Woo, additional, Laganowsky, Arthur D., additional, Rodriguez, Jose, additional, Burghammer, Manfred, additional, Shoeman, Robert L., additional, Doak, R. Bruce, additional, Weik, Martin, additional, Sauter, Nicholas K., additional, Federici, Brian, additional, Cascio, Duilio, additional, Schlichting, Ilme, additional, and Colletier, Jacques-Philippe, additional
- Published
- 2021
- Full Text
- View/download PDF
35. Rational control of structural off-state heterogeneity in a photoswitchable fluorescent protein provides switching contrast enhancement
- Author
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Adam, Virgile, primary, Hadjidemetriou, Kyprianos, additional, Jensen, Nickels, additional, Shoeman, Robert L., additional, Woodhouse, Joyce, additional, Aquila, Andrew, additional, Banneville, Anne-Sophie, additional, Barends, Thomas R. M., additional, Bezchastnov, Victor, additional, Boutet, Sébastien, additional, Byrdin, Martin, additional, Cammarata, Marco, additional, Carbajo, Sergio, additional, Christou, Nina Eleni, additional, Coquelle, Nicolas, additional, De la Mora, Eugenio, additional, El Khatib, Mariam, additional, Chicano, Tadeo Moreno, additional, Doak, R. Bruce, additional, Fieschi, Franck, additional, Foucar, Lutz, additional, Glushonkov, Oleksandr, additional, Gorel, Alexander, additional, Grünbein, Marie Luise, additional, Hilpert, Mario, additional, Hunter, Mark, additional, Kloos, Marco, additional, Koglin, Jason E., additional, Lane, Thomas J., additional, Liang, Mengning, additional, Mantovanelli, Angela, additional, Nass, Karol, additional, Kovacs, Gabriela Nass, additional, Owada, Shigeki, additional, Roome, Christopher M., additional, Schirò, Giorgio, additional, Seaberg, Matthew, additional, Stricker, Miriam, additional, Thépaut, Michel, additional, Tono, Kensuke, additional, Ueda, Kiyoshi, additional, Uriarte, Lucas M., additional, You, Daehyun, additional, Zala, Ninon, additional, Domratcheva, Tatiana, additional, Jakobs, Stefan, additional, Sliwa, Michel, additional, Schlichting, Ilme, additional, Colletier, Jacques-Philippe, additional, Bourgeois, Dominique, additional, and Weik, Martin, additional
- Published
- 2021
- Full Text
- View/download PDF
36. Data reduction for serial crystallography using a robust peak finder
- Author
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Hadian-Jazi, Marjan, primary, Sadri, Alireza, additional, Barty, Anton, additional, Yefanov, Oleksandr, additional, Galchenkova, Marina, additional, Oberthuer, Dominik, additional, Komadina, Dana, additional, Brehm, Wolfgang, additional, Kirkwood, Henry, additional, Mills, Grant, additional, de Wijn, Raphael, additional, Letrun, Romain, additional, Kloos, Marco, additional, Vakili, Mohammad, additional, Gelisio, Luca, additional, Darmanin, Connie, additional, Mancuso, Adrian P., additional, Chapman, Henry N., additional, and Abbey, Brian, additional
- Published
- 2021
- Full Text
- View/download PDF
37. Structure and allosteric regulation of eukaryotic 6-phosphofructokinases
- Author
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Schöneberg, Torsten, Kloos, Marco, Brüser, Antje, Kirchberger, Jürgen, and Sträter, Norbert
- Published
- 2013
- Full Text
- View/download PDF
38. Observation of shock-induced protein crystal damage during megahertz serial femtosecond crystallography
- Author
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Grünbein, Marie L., primary, Foucar, Lutz, additional, Gorel, Alexander, additional, Hilpert, Mario, additional, Kloos, Marco, additional, Nass, Karol, additional, Kovacs, Gabriela Nass, additional, Roome, Christopher M., additional, Shoeman, Robert L., additional, Stricker, Miriam, additional, Carbajo, Sergio, additional, Colocho, William, additional, Gilevich, Sasha, additional, Hunter, Mark, additional, Lewandowski, Jim, additional, Lutman, Alberto, additional, Koglin, Jason E., additional, Lane, Thomas J., additional, van Driel, Tim, additional, Sheppard, John, additional, Vetter, Sharon L., additional, Turner, James L., additional, Doak, R. Bruce, additional, Barends, Thomas R. M., additional, Boutet, Sébastien, additional, Aquila, Andrew L., additional, Decker, Franz-Josef, additional, Schlichting, Ilme, additional, and Stan, Claudiu A., additional
- Published
- 2021
- Full Text
- View/download PDF
39. Shock Damage Analysis in Serial Femtosecond Crystallography Data Collected at MHz X-ray Free-Electron Lasers
- Author
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Gorel, Alexander, primary, Grünbein, Marie, additional, Bean, Richard, additional, Bielecki, Johan, additional, Hilpert, Mario, additional, Cascella, Michele, additional, Colletier, Jacques-Philippe, additional, Fangohr, Hans, additional, Foucar, Lutz, additional, Hartmann, Elisabeth, additional, Hunter, Mark, additional, Kirkwood, Henry, additional, Kloos, Marco, additional, Letrun, Romain, additional, Michelat, Thomas, additional, Shoeman, Robert, additional, Sztuk-Dambietz, Jolanta, additional, Tetreau, Guillaume, additional, Zimmermann, Herbert, additional, Mancuso, Adrian, additional, Barends, Thomas, additional, Doak, R., additional, Stan, Claudiu, additional, and Schlichting, Ilme, additional
- Published
- 2020
- Full Text
- View/download PDF
40. Direct Observation of the Mechanism of Antibiotic Resistance by Mix-and-Inject at the European XFEL
- Author
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Pandey, Suraj, primary, Calvey, George, additional, Katz, Andrea M., additional, Malla, Tek Narsingh, additional, Koua, Faisal H. M., additional, Martin-Garcia, Jose M., additional, Poudyal, Ishwor, additional, Yang, Jay-How, additional, Vakili, Mohammad, additional, Yefanov, Oleksandr, additional, Zielinski, Kara A., additional, Bajt, Saša, additional, Awel, Salah, additional, Dörner, Katerina, additional, Frank, Matthias, additional, Gelisio, Luca, additional, Jernigan, Rebecca, additional, Kirkwood, Henry, additional, Kloos, Marco, additional, Koliyadu, Jayanath, additional, Mariani, Valerio, additional, Miller, Mitchell D., additional, Mills, Grant, additional, Nelson, Garrett, additional, Olmos, Jose L., additional, Sadri, Alireza, additional, Sato, Tokushi, additional, Tolstikova, Alexandra, additional, Xu, Weijun, additional, Ourmazd, Abbas, additional, Spence, John H. C., additional, Schwander, Peter, additional, Barty, Anton, additional, Chapman, Henry N., additional, Fromme, Petra, additional, Mancuso, Adrian P., additional, Phillips, George N., additional, Bean, Richard, additional, Pollack, Lois, additional, and Schmidt, Marius, additional
- Published
- 2020
- Full Text
- View/download PDF
41. Current status and future opportunities for serial crystallography at MAX IV Laboratory
- Author
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Shilova, Anastasya, primary, Lebrette, Hugo, additional, Aurelius, Oskar, additional, Nan, Jie, additional, Welin, Martin, additional, Kovacic, Rebeka, additional, Ghosh, Swagatha, additional, Safari, Cecilia, additional, Friel, Ross J., additional, Milas, Mirko, additional, Matej, Zdenek, additional, Högbom, Martin, additional, Brändén, Gisela, additional, Kloos, Marco, additional, Shoeman, Robert L., additional, Doak, Bruce, additional, Ursby, Thomas, additional, Håkansson, Maria, additional, Logan, Derek T., additional, and Mueller, Uwe, additional
- Published
- 2020
- Full Text
- View/download PDF
42. BioMAX – the first macromolecular crystallography beamline at MAX IV Laboratory
- Author
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Ursby, Thomas, primary, Åhnberg, Karl, additional, Appio, Roberto, additional, Aurelius, Oskar, additional, Barczyk, Artur, additional, Bartalesi, Antonio, additional, Bjelčić, Monika, additional, Bolmsten, Fredrik, additional, Cerenius, Yngve, additional, Doak, R. Bruce, additional, Eguiraun, Mikel, additional, Eriksson, Thomas, additional, Friel, Ross J., additional, Gorgisyan, Ishkhan, additional, Gross, Andrea, additional, Haghighat, Vahid, additional, Hennies, Franz, additional, Jagudin, Elmir, additional, Norsk Jensen, Brian, additional, Jeppsson, Tobias, additional, Kloos, Marco, additional, Lidon-Simon, Julio, additional, de Lima, Gustavo M. A., additional, Lizatovic, Robert, additional, Lundin, Magnus, additional, Milan-Otero, Antonio, additional, Milas, Mirko, additional, Nan, Jie, additional, Nardella, Alberto, additional, Rosborg, Anders, additional, Shilova, Anastasya, additional, Shoeman, Robert L., additional, Siewert, Frank, additional, Sondhauss, Peter, additional, Talibov, Vladimir O., additional, Tarawneh, Hamed, additional, Thånell, Johan, additional, Thunnissen, Marjolein, additional, Unge, Johan, additional, Ward, Christopher, additional, Gonzalez, Ana, additional, and Mueller, Uwe, additional
- Published
- 2020
- Full Text
- View/download PDF
43. Current status and future opportunities for serial crystallography at MAX IV Laboratory
- Author
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Shilova, Anastasya, Lebrette, Hugo, Aurelius, Oskar, Nan, Jie, Welin, Martin, Kovacic, Rebeka, Ghosh, Swagatha, Safari, Cecilia, Friel, Ross J., Milas, Mirko, Matej, Zdenek, Högbom, Martin, Brändén, Gisela, Kloos, Marco, Shoeman, Robert L., Doak, Bruce, Ursby, Thomas, Håkansson, Maria, Logan, Derek T., Mueller, Uwe, Shilova, Anastasya, Lebrette, Hugo, Aurelius, Oskar, Nan, Jie, Welin, Martin, Kovacic, Rebeka, Ghosh, Swagatha, Safari, Cecilia, Friel, Ross J., Milas, Mirko, Matej, Zdenek, Högbom, Martin, Brändén, Gisela, Kloos, Marco, Shoeman, Robert L., Doak, Bruce, Ursby, Thomas, Håkansson, Maria, Logan, Derek T., and Mueller, Uwe
- Abstract
Over the last decade, serial crystallography, a method to collect complete diffraction datasets from a large number of microcrystals delivered and exposed to an X-ray beam in random orientations at room temperature, has been successfully implemented at X-ray free-electron lasers and synchrotron radiation facility beamlines. This development relies on a growing variety of sample presentation methods, including different fixed target supports, injection methods using gas-dynamic virtual-nozzle injectors and high-viscosity extrusion injectors, and acoustic levitation of droplets, each with unique requirements. In comparison with X-ray free-electron lasers, increased beam time availability makes synchrotron facilities very attractive to perform serial synchrotron X-ray crystallography (SSX) experiments. Within this work, the possibilities to perform SSX at BioMAX, the first macromolecular crystallography beamline at studies from the SSX user program: an implementation of a high-viscosity extrusion injector to perform room temperature serial crystallography at BioMAX using two solid supports - silicon nitride membranes (Silson, UK) and XtalTool (Jena Bioscience, Germany). Future perspectives for the dedicated serial crystallography beamline MicroMAX at MAX IV Laboratory, which will provide parallel and intense micrometre-sized X-ray beams, are discussed.
- Published
- 2020
- Full Text
- View/download PDF
44. Well-based crystallization of lipidic cubic phase microcrystals for serial X-ray crystallography experiments
- Author
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Andersson, Rebecka, primary, Safari, Cecilia, additional, Båth, Petra, additional, Bosman, Robert, additional, Shilova, Anastasya, additional, Dahl, Peter, additional, Ghosh, Swagatha, additional, Dunge, Andreas, additional, Kjeldsen-Jensen, Rasmus, additional, Nan, Jie, additional, Shoeman, Robert L., additional, Kloos, Marco, additional, Doak, R. Bruce, additional, Mueller, Uwe, additional, Neutze, Richard, additional, and Brändén, Gisela, additional
- Published
- 2019
- Full Text
- View/download PDF
45. Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin
- Author
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Nass Kovacs, Gabriela, primary, Colletier, Jacques-Philippe, additional, Grünbein, Marie Luise, additional, Yang, Yang, additional, Stensitzki, Till, additional, Batyuk, Alexander, additional, Carbajo, Sergio, additional, Doak, R. Bruce, additional, Ehrenberg, David, additional, Foucar, Lutz, additional, Gasper, Raphael, additional, Gorel, Alexander, additional, Hilpert, Mario, additional, Kloos, Marco, additional, Koglin, Jason E., additional, Reinstein, Jochen, additional, Roome, Christopher M., additional, Schlesinger, Ramona, additional, Seaberg, Matthew, additional, Shoeman, Robert L., additional, Stricker, Miriam, additional, Boutet, Sébastien, additional, Haacke, Stefan, additional, Heberle, Joachim, additional, Heyne, Karsten, additional, Domratcheva, Tatiana, additional, Barends, Thomas R. M., additional, and Schlichting, Ilme, additional
- Published
- 2019
- Full Text
- View/download PDF
46. Crystallography on a chip – without the chip: sheet-on-sheet sandwich
- Author
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Doak, R. Bruce, primary, Nass Kovacs, Gabriela, additional, Gorel, Alexander, additional, Foucar, Lutz, additional, Barends, Thomas R. M., additional, Grünbein, Marie Luise, additional, Hilpert, Mario, additional, Kloos, Marco, additional, Roome, Christopher M., additional, Shoeman, Robert L., additional, Stricker, Miriam, additional, Tono, Kensuke, additional, You, Daehyun, additional, Ueda, Kiyoshi, additional, Sherrell, Darren A., additional, Owen, Robin L., additional, and Schlichting, Ilme, additional
- Published
- 2018
- Full Text
- View/download PDF
47. Two-colour serial femtosecond crystallography dataset from gadoteridol-derivatized lysozyme for MAD phasing
- Author
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Gorel, Alexander, primary, Motomura, Koji, additional, Fukuzawa, Hironobu, additional, Doak, R. Bruce, additional, Grünbein, Marie Luise, additional, Hilpert, Mario, additional, Inoue, Ichiro, additional, Kloos, Marco, additional, Nass Kovács, Gabriela, additional, Nango, Eriko, additional, Nass, Karol, additional, Roome, Christopher M, additional, Shoeman, Robert L, additional, Tanaka, Rie, additional, Tono, Kensuke, additional, Foucar, Lutz, additional, Joti, Yasumasa, additional, Yabashi, Makina, additional, Iwata, So, additional, Ueda, Kiyoshi, additional, Barends, Thomas R. M, additional, and Schlichting, Ilme, additional
- Published
- 2017
- Full Text
- View/download PDF
48. Multi-wavelength anomalous diffraction de novo phasing using a two-colour X-ray free-electron laser with wide tunability
- Author
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Gorel, Alexander, primary, Motomura, Koji, additional, Fukuzawa, Hironobu, additional, Doak, R. Bruce, additional, Grünbein, Marie Luise, additional, Hilpert, Mario, additional, Inoue, Ichiro, additional, Kloos, Marco, additional, Kovácsová, Gabriela, additional, Nango, Eriko, additional, Nass, Karol, additional, Roome, Christopher M., additional, Shoeman, Robert L., additional, Tanaka, Rie, additional, Tono, Kensuke, additional, Joti, Yasumasa, additional, Yabashi, Makina, additional, Iwata, So, additional, Foucar, Lutz, additional, Ueda, Kiyoshi, additional, Barends, Thomas R. M., additional, and Schlichting, Ilme, additional
- Published
- 2017
- Full Text
- View/download PDF
49. Viscous hydrophilic injection matrices for serial crystallography
- Author
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Kovácsová, Gabriela, primary, Grünbein, Marie Luise, additional, Kloos, Marco, additional, Barends, Thomas R. M., additional, Schlesinger, Ramona, additional, Heberle, Joachim, additional, Kabsch, Wolfgang, additional, Shoeman, Robert L., additional, Doak, R. Bruce, additional, and Schlichting, Ilme, additional
- Published
- 2017
- Full Text
- View/download PDF
50. Crystal structure of human platelet phosphofructokinase-1 locked in an activated conformation
- Author
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Kloos, Marco, primary, Brüser, Antje, additional, Kirchberger, Jürgen, additional, Schöneberg, Torsten, additional, and Sträter, Norbert, additional
- Published
- 2015
- Full Text
- View/download PDF
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