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1. Microsecond time-resolved X-ray scattering by utilizing MHz repetition rate at second-generation XFELs

Author

Konold, Patrick E., Monrroy, Leonardo, Bellisario, Alfredo, Filipe, Diogo, Adams, Patrick, Alvarez, Roberto, Bean, Richard, Bielecki, Johan, Bódizs, Szabolcs, Ducrocq, Gabriel, Grubmueller, Helmut, Kirian, Richard A., Kloos, Marco, Koliyadu, Jayanath C. P., Koua, Faisal H. M., Larkiala, Taru, Letrun, Romain, Lindsten, Fredrik, Maihöfer, Michael, Martin, Andrew V., Mészáros, Petra, Mutisya, Jennifer, Nimmrich, Amke, Okamoto, Kenta, Round, Adam, Sato, Tokushi, Valerio, Joana, Westphal, Daniel, Wollter, August, Yenupuri, Tej Varma, You, Tong, Maia, Filipe, and Westenhoff, Sebastian

Published
2024
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2. 3D-Printed Sheet Jet for Stable Megahertz Liquid Sample Delivery at X-ray Free Electron Lasers

Author

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.

Subjects
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.

Published
2023
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3. SARS-CoV-2 Mpro responds to oxidation by forming disulfide and NOS/SONOS bonds

Author

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.

Published
2024
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4. Influence of pump laser fluence on ultrafast myoglobin structural dynamics

Author

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

Published
2024
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5. Rational Control of Off‐State Heterogeneity in a Photoswitchable Fluorescent Protein Provides Switching Contrast Enhancement**

Author

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

Subjects
Generic health relevance, 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
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.

Published
2022

6. Form factor determination of biological molecules with X-ray free electron laser small-angle scattering (XFEL-SAS)

Author

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

Published
2023
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7. Co-flow injection for serial crystallography at X-ray free-electron lasers.

Author

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

Subjects
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.

Published
2022

8. De novo determination of mosquitocidal Cry11Aa and Cry11Ba structures from naturally-occurring nanocrystals

Author

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

Subjects
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.

Published
2022

9. Observation of substrate diffusion and ligand binding in enzyme crystals using high-repetition-rate mix-and-inject serial crystallography

Author

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

Subjects
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.

Published
2021

10. De novo determination of mosquitocidal Cry11Aa and Cry11Ba structures from naturally-occurring nanocrystals

Author

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

Subjects
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

11. Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin

Author

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

Subjects
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.

Published
2019
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12. A multi-million image Serial Femtosecond Crystallography dataset collected at the European XFEL

Author

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.

Published
2022
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13. Crystal structure of a bacterial photoactivated adenylate cyclase determined at room temperature by serial femtosecond crystallography

Author

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

Published
2024
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15. Insights into an efficient light-driven hybrid P450 BM3 enzyme from crystallographic, spectroscopic and biochemical studies

Author

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

Subjects
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.

Published
2016

16. Microsecond time-resolved X-ray scattering by utilizing MHz repetition rate at second-generation XFELs

Author

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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17. Structure of the Lysinibacillus sphaericus Tpp49Aa1 pesticidal protein elucidated from natural crystals using MHz-SFX

Author

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
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18. Effect of X-ray free-electron laser-induced shockwaves on haemoglobin microcrystals delivered in a liquid jet

Author

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

Published
2021
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20. 3D-printed sheet jet for stable megahertz liquid sample delivery at X-ray free-electron lasers

Author

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
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22. Structural dynamics in proteins induced by and probed with X-ray free-electron laser pulses

Author

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
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23. XFEL Microcrystallography of Self-Assembling Silver n-Alkanethiolates

Author

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
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24. Mix-and-extrude: high-viscosity sample injection towards time-resolved protein crystallography

Author

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
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25. Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin

Author

Nass Kovacs, Gabriela, Colletier, Jacques-Philippe, Grünbein, Marie Luise, Yang, Yang, Stensitzki, Till, Batyuk, Alexander, Carbajo, Sergio, Doak, R. Bruce, Ehrenberg, David, Foucar, Lutz, Gasper, Raphael, Gorel, Alexander, Hilpert, Mario, Kloos, Marco, Koglin, Jason E., Reinstein, Jochen, Roome, Christopher M., Schlesinger, Ramona, Seaberg, Matthew, Shoeman, Robert L., Stricker, Miriam, Boutet, Sébastien, Haacke, Stefan, Heberle, Joachim, Heyne, Karsten, Domratcheva, Tatiana, Barends, Thomas R. M., and Schlichting, Ilme

Published
2019
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26. MHz data collection of a microcrystalline mixture of different jack bean proteins

Author

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
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28. Influence of pump laser fluence on ultrafast structural changes in myoglobin

Author

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
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29. Cover Feature: Rational Control of Off‐State Heterogeneity in a Photoswitchable Fluorescent Protein Provides Switching Contrast Enhancement (ChemPhysChem 19/2022)

Author

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
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30. Megahertz data collection from protein microcrystals at an X-ray free-electron laser

Author

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
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31. 3D printed devices and infrastructure for liquid sample delivery at the European XFEL

Author

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
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32. Structure of the Lysinibacillus sphaericus Tpp49Aa1 pesticidal protein elucidated from natural crystals using MHz-SFX

Author

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
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33. De novo determination of mosquitocidal Cry11Aa and Cry11Ba structures from naturally-occurring nanocrystals

Author

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
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34. Rational control of structural off-state heterogeneity in a photoswitchable fluorescent protein provides switching contrast enhancement

Author

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
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35. Data reduction for serial crystallography using a robust peak finder

Author

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
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36. Current status and future opportunities for serial crystallography at MAX IV Laboratory

Author

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
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37. Observation of shock-induced protein crystal damage during megahertz serial femtosecond crystallography

Author

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
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38. Shock Damage Analysis in Serial Femtosecond Crystallography Data Collected at MHz X-ray Free-Electron Lasers

Author

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
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39. Direct Observation of the Mechanism of Antibiotic Resistance by Mix-and-Inject at the European XFEL

Author

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
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41. Current status and future opportunities for serial crystallography at MAX IV Laboratory

Author

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
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42. BioMAX – the first macromolecular crystallography beamline at MAX IV Laboratory

Author

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
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43. Well-based crystallization of lipidic cubic phase microcrystals for serial X-ray crystallography experiments

Author

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
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44. Crystallography on a chip – without the chip: sheet-on-sheet sandwich

Author

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
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45. Two-colour serial femtosecond crystallography dataset from gadoteridol-derivatized lysozyme for MAD phasing

Author

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
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46. Multi-wavelength anomalous diffraction de novo phasing using a two-colour X-ray free-electron laser with wide tunability

Author

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
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47. Viscous hydrophilic injection matrices for serial crystallography

Author

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
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