130 results on '"Fromme, Raimund"'
Search Results
102. S2.11 Structure of photosystem I and its natural electron acceptor ferredoxin in co-crystals at 3.8 Å resolution
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Fromme, Raimund, primary, Yu, Hongqi, additional, Jolley, Craig, additional, Grotjohann, Ingo, additional, Wang, Meitian, additional, Sétif, Pierre, additional, Bottin, Hervé, additional, and Fromme, Petra, additional
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- 2008
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103. Crystallization of the c14-rotor of the chloroplast ATP synthase reveals that it contains pigments
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Varco-Merth, Benjamin, primary, Fromme, Raimund, additional, Wang, Meitian, additional, and Fromme, Petra, additional
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- 2008
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104. Conformational gating of dimannose binding to the antiviral protein cyanovirin revealed from the crystal structure at 1.35 Å resolution
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Fromme, Raimund, primary, Katiliene, Zivile, additional, Fromme, Petra, additional, and Ghirlanda, Giovanna, additional
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- 2008
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105. A Monovalent Mutant of Cyanovirin-N Provides Insight into the Role of Multiple Interactions with gp120 for Antiviral Activity,
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Fromme, Raimund, primary, Katiliene, Zivile, additional, Giomarelli, Barbara, additional, Bogani, Federica, additional, Mc Mahon, James, additional, Mori, Toshiyuki, additional, Fromme, Petra, additional, and Ghirlanda, Giovanna, additional
- Published
- 2007
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106. Microsecond Time Scale Rotation Measurements of Single F1-ATPase Molecules
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Spetzler, David, primary, York, Justin, additional, Daniel, Douglas, additional, Fromme, Raimund, additional, Lowry, David, additional, and Frasch, Wayne, additional
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- 2006
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107. Acid-Base Catalysis and Crystal Structures of a Least Evolved Ancestral GFP-like Protein Undergoing Green-to-Red Photoconversion.
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Hanseong Kim, Gnmkemeyer, Timothy J., Modi, Chintan, Liqing Chen, Fromme, Raimund, Matz, Mikhail V., and Wachter, Rebekka M.
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- 2013
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108. Crystallization of the c14-rotor of the chloroplast ATP synthase reveals that it contains pigments
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Varco-Merth, Benjamin, Fromme, Raimund, Wang, Meitian, and Fromme, Petra
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CRYSTALLIZATION , *CHLOROPLASTS , *BIOLOGICAL pigments , *PROTON transfer reactions - Abstract
Abstract: The ATP synthase is one of the most important enzymes on earth as it couples the transmembrane electrochemical potential of protons to the synthesis of ATP from ADP and inorganic phosphate, providing the main ATP source of almost all higher life on earth. During ATP synthesis, stepwise protonation of a conserved carboxylate on each protein subunit of an oligomeric ring of 10–15 c-subunits is commonly thought to drive rotation of the rotor moiety (c10–14γɛ) relative to stator moiety (α3β3δab2). Here we report the isolation and crystallization of the c14-ring of subunit c from the spinach chloroplast enzyme diffracting as far as 2.8 Å. Though ATP synthase was not previously known to contain any pigments, the crystals of the c-subunit possessed a strong yellow color. The pigment analysis revealed that they contain 1 chlorophyll and 2 carotenoids, thereby showing for the first time that the chloroplast ATP synthase contains cofactors, leading to the question of the possible roles of the functions of the pigments in the chloroplast ATP synthase. [Copyright &y& Elsevier]
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- 2008
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109. Microsecond Time Scale Rotation Measurements of Single F1-ATPase Molecules.
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Spetzler, David, York, Justin, Daniel, Douglas, Fromme, Raimund, Lowry, David, and Frasch, Wayne
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- 2006
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110. Structural enzymology using X-ray free electron lasers
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Kupitz, Christopher, Olmos, Jose L., Holl, Mark, Tremblay, Lee, Pande, Kanupriya, Pandey, Suraj, Oberthür, Dominik, Hunter, Mark, Liang, Mengning, Aquila, Andrew, Tenboer, Jason, Calvey, George, Katz, Andrea, Chen, Yujie, Wiedorn, Max O., Knoska, Juraj, Meents, Alke, Majriani, Valerio, Norwood, Tyler, Poudyal, Ishwor, Grant, Thomas, Miller, Mitchell D., Xu, Weijun, Tolstikova, Aleksandra, Morgan, Andrew, Metz, Markus, Martin-Gracia, Jose, Zook, James D., Roy-Chowdhury, Shatabdi, Coe, Jesse, Nagaratnam, Nirupa, Meza, Domingo, Fromme, Raimund, Basu, Shibom, Frank, Matthias, White, Thomas, Barty, Anton, Bajt, Sasa, Yefanov, Oleksandr, Chapman, Henry N., Zatsepin, Nadia, Nelson, Garrett, Weierstall, Uwe, Spence, John, Schwander, Peter, Pollack, Lois, Fromme, Petra, Ourmazd, Abbas, Phillips, George N., and Schmidt, Marius
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3. Good health - Abstract
Structural dynamics 4(4), 044003 (2017). doi:10.1063/1.4972069, Mix-and-inject serial crystallography (MISC) is a technique designed to image enzyme catalyzed reactions in which small protein crystals are mixed with a substrate just prior to being probed by an X-ray pulse. This approach offers several advantages over flow cell studies. It provides (i) room temperature structures at near atomic resolution, (ii) time resolution ranging from microseconds to seconds, and (iii) convenient reaction initiation. It outruns radiation damage by using femtosecond X-ray pulses allowing damage and chemistry to be separated. Here, we demonstrate that MISC is feasible at an X-ray free electron laser by studying the reaction of M. tuberculosis ß-lactamase microcrystals with ceftriaxone antibiotic solution. Electron density maps of the apo-ß-lactamase and of the ceftriaxone bound form were obtained at 2.8 Å and 2.4 Å resolution, respectively. These results pave the way to study cyclic and non-cyclic reactions and represent a new field of time-resolved structural dynamics for numerous substrate-triggered biological reactions., Published by AIP Publishing LLC, Melville, NY
111. Ternary structure reveals mechanism of a membrane diacylglycerol kinase
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Li, Dianfan, Stansfeld, Phillip J., Sansom, Mark S. P., Keogh, Aaron, Vogeley, Lutz, Howe, Nicole, Lyons, Joseph A., Aragao, David, Fromme, Petra, Fromme, Raimund, Basu, Shibom, Grotjohann, Ingo, Kupitz, Christopher, Rendek, Kimberley, Weierstall, Uwe, Zatsepin, Nadia A., Cherezov, Vadim, Liu, Wei, Bandaru, Sateesh, English, Niall J., Gati, Cornelius, Barty, Anton, Yefanov, Oleksandr, Chapman, Henry N., Diederichs, Kay, Messerschmidt, Marc, Boutet, Sébastien, Williams, Garth J., Marvin Seibert, M., and Caffrey, Martin
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3. Good health - Abstract
Nature Communications 6, 10140 (2015). doi:10.1038/ncomms10140, iacylglycerol kinase catalyses the ATP-dependent conversion of diacylglycerol to phosphatidic acid in the plasma membrane of Escherichia coli. The small size of this integral membrane trimer, which has 121 residues per subunit, means that available protein must be used economically to craft three catalytic and substrate-binding sites centred about the membrane/cytosol interface. How nature has accomplished this extraordinary feat is revealed here in a crystal structure of the kinase captured as a ternary complex with bound lipid substrate and an ATP analogue. Residues, identified as essential for activity by mutagenesis, decorate the active site and are rationalized by the ternary structure. The γ-phosphate of the ATP analogue is positioned for direct transfer to the primary hydroxyl of the lipid whose acyl chain is in the membrane. A catalytic mechanism for this unique enzyme is proposed. The active site architecture shows clear evidence of having arisen by convergent evolution., Published by Nature Publishing Group, London
112. In cellulo crystallization of Trypanosoma brucei IMP dehydrogenase enables the identification of genuine co-factors
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Nass, Karol, Redecke, Lars, Perbandt, Markus, Yefanov, O., Klinge, M., Koopmann, R., Stellato, F., Gabdulkhakov, A., Schönherr, R., Rehders, D., Lahey-Rudolph, J. M., Aquila, A., Barty, A., Basu, Shibom, Doak, R. Bruce, Duden, R., Frank, Matthias, Fromme, Raimund, Kassemeyer, S., Katona, Gergely, Kirian, Richard, Liu, H., Majoul, I., Martin-Garcia, J. M., Messerschmidt, M., Shoeman, R. L., Weierstall, U., Westenhoff, S., White, Thomas, Williams, G. J., Yoon, C. H., Zatsepin, Nadia, Fromme, P., Duszenko, M., Chapman, H. N., and Betzel, C.
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3. Good health - Abstract
Nature Communications 11(1), 620 (2020). doi:10.1038/s41467-020-14484-w, Sleeping sickness is a fatal disease caused by the protozoan parasite Trypanosoma brucei (Tb). Inosine-5’-monophosphate dehydrogenase (IMPDH) has been proposed as a potential drug target, since it maintains the balance between guanylate deoxynucleotide and ribonucleotide levels that is pivotal for the parasite. Here we report the structure of TbIMPDH at room temperature utilizing free-electron laser radiation on crystals grown in living insect cells. The 2.80 Å resolution structure reveals the presence of ATP and GMP at the canonical sites of the Bateman domains, the latter in a so far unknown coordination mode. Consistent with previously reported IMPDH complexes harboring guanosine nucleotides at the second canonical site, TbIMPDH forms a compact oligomer structure, supporting a nucleotide-controlled conformational switch that allosterically modulates the catalytic activity. The oligomeric TbIMPDH structure we present here reveals the potential of in cellulo crystallization to identify genuine allosteric co-factors from a natural reservoir of specific compounds., Published by Nature Publishing Group UK, [London]
113. Enzyme intermediates captured 'on the fly' by mix-and-inject serial crystallography
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Olmos, Jose L., Pandey, Suraj, Martin-Garcia, Jose M., Calvey, George, Katz, Andrea, Knoska, Juraj, Kupitz, Christopher, Hunter, Mark S., Liang, Mengning, Oberthuer, Dominik, Yefanov, Oleksandr, Wiedorn, Max, Heyman, Michael, Holl, Mark, Pande, Kanupriya, Barty, Anton, Miller, Mitchell D., Stern, Stephan, Roy-Chowdhury, Shatabdi, Coe, Jesse, Nagaratnam, Nirupa, Zook, James, Verburgt, Jacob, Norwood, Tyler, Poudyal, Ishwor, Xu, David, Koglin, Jason, Seaberg, Matthew H., Zhao, Yun, Bajt, Saša, Grant, Thomas, Mariani, Valerio, Nelson, Garrett, Subramanian, Ganesh, Bae, Euiyoung, Fromme, Raimund, Fung, Russell, Schwander, Peter, Frank, Matthias, White, Thomas A., Weierstall, Uwe, Zatsepin, Nadia, Spence, John, Fromme, Petra, Chapman, Henry N., Pollack, Lois, Tremblay, Lee, Ourmazd, Abbas, Phillips, George N., and Schmidt, Marius
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3. Good health - Abstract
BMC biology 16(1), 59 (2018). doi:10.1186/s12915-018-0524-5, Published by Springer, Berlin
114. Isolation and characterization of the F1F0 ATP synthase from Heliobacterium modesticaldum.
- Author
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Yang, Jay-How, Fromme, Raimund, Fromme, Petra, Redding, Kevin, Sarrous, Iosifina, and Evans, James E.
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- 2014
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115. X-ray crystal structure of the passenger domain of plasmid encoded toxin(Pet), an autotransporter enterotoxin from enteroaggregative Escherichia coli (EAEC)
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Fromme, Raimund
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- 2014
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116. Detection of a Geminate Photoproduct of Bovine Cytochrome c Oxidase by Time-Resolved Serial Femtosecond Crystallography.
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Ishigami I, Carbajo S, Zatsepin N, Hikita M, Conrad CE, Nelson G, Coe J, Basu S, Grant T, Seaberg MH, Sierra RG, Hunter MS, Fromme P, Fromme R, Rousseau DL, and Yeh SR
- Subjects
- Cattle, Animals, Oxidation-Reduction, Ligands, Oxygen chemistry, Crystallography, X-Ray, Iron chemistry, Water metabolism, Electron Transport Complex IV chemistry, Copper chemistry
- Abstract
Cytochrome c oxidase (C c O) is a large membrane-bound hemeprotein that catalyzes the reduction of dioxygen to water. Unlike classical dioxygen binding hemeproteins with a heme b group in their active sites, C c O has a unique binuclear center (BNC) composed of a copper atom (Cu
B ) and a heme a3 iron, where O2 binds and is reduced to water. CO is a versatile O2 surrogate in ligand binding and escape reactions. Previous time-resolved spectroscopic studies of the CO complexes of bovine C c O (bC c O) revealed that photolyzing CO from the heme a3 iron leads to a metastable intermediate (CuB -CO), where CO is bound to CuB , before it escapes out of the BNC. Here, with a pump-probe based time-resolved serial femtosecond X-ray crystallography, we detected a geminate photoproduct of the bC c O-CO complex, where CO is dissociated from the heme a3 iron and moved to a temporary binding site midway between the CuB and the heme a3 iron, while the locations of the two metal centers and the conformation of Helix-X, housing the proximal histidine ligand of the heme a3 iron, remain in the CO complex state. This new structure, combined with other reported structures of bC c O, allows for a clearer definition of the ligand dissociation trajectory as well as the associated protein dynamics.- Published
- 2023
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117. Room-temperature structural studies of SARS-CoV-2 protein NendoU with an X-ray free-electron laser.
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Jernigan RJ, Logeswaran D, Doppler D, Nagaratnam N, Sonker M, Yang JH, Ketawala G, Martin-Garcia JM, Shelby ML, Grant TD, Mariani V, Tolstikova A, Sheikh MZ, Yung MC, Coleman MA, Zaare S, Kaschner EK, Rabbani MT, Nazari R, Zacks MA, Hayes B, Sierra RG, Hunter MS, Lisova S, Batyuk A, Kupitz C, Boutet S, Hansen DT, Kirian RA, Schmidt M, Fromme R, Frank M, Ros A, Chen JJ, Botha S, and Fromme P
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- Humans, Crystallography, X-Ray, Temperature, Electrons, Lasers, SARS-CoV-2, COVID-19
- Abstract
NendoU from SARS-CoV-2 is responsible for the virus's ability to evade the innate immune system by cleaving the polyuridine leader sequence of antisense viral RNA. Here we report the room-temperature structure of NendoU, solved by serial femtosecond crystallography at an X-ray free-electron laser to 2.6 Å resolution. The room-temperature structure provides insight into the flexibility, dynamics, and other intrinsic properties of NendoU, with indications that the enzyme functions as an allosteric switch. Functional studies examining cleavage specificity in solution and in crystals support the uridine-purine cleavage preference, and we demonstrate that enzyme activity is fully maintained in crystal form. Optimizing the purification of NendoU and identifying suitable crystallization conditions set the benchmark for future time-resolved serial femtosecond crystallography studies. This could advance the design of antivirals with higher efficacy in treating coronaviral infections, since drugs that block allosteric conformational changes are less prone to drug resistance., Competing Interests: Declaration of interests The authors declare no competing interests., (Copyright © 2022. Published by Elsevier Ltd.)
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- 2023
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118. Co-flow injection for serial crystallography at X-ray free-electron lasers.
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Doppler D, Rabbani MT, Letrun R, Cruz Villarreal J, Kim DH, Gandhi S, Egatz-Gomez A, Sonker M, Chen J, Koua FHM, Yang J, Youssef M, Mazalova V, Bajt S, Shelby ML, Coleman MA, Wiedorn MO, Knoska J, Schön S, Sato T, Hunter MS, Hosseinizadeh A, Kuptiz C, Nazari R, Alvarez RC, Karpos K, Zaare S, Dobson Z, Discianno E, Zhang S, Zook JD, Bielecki J, de Wijn R, Round AR, Vagovic P, Kloos M, Vakili M, Ketawala GK, Stander NE, Olson TL, Morin K, Mondal J, Nguyen J, Meza-Aguilar JD, Kodis G, Vaiana S, Martin-Garcia JM, Mariani V, Schwander P, Schmidt M, Messerschmidt M, Ourmazd A, Zatsepin N, Weierstall U, Bruce BD, Mancuso AP, Grant T, Barty A, Chapman HN, Frank M, Fromme R, Spence JCH, Botha S, Fromme P, Kirian RA, and Ros A
- 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., (© Diandra Doppler et al. 2022.)
- Published
- 2022
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119. Author Correction: Membrane protein megahertz crystallography at the European XFEL.
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Gisriel C, Coe J, Letrun R, Yefanov OM, Luna-Chavez C, Stander NE, Lisova S, Mariani V, Kuhn M, Aplin S, Grant TD, Dörner K, Sato T, Echelmeier A, Villarreal JC, Hunter MS, Wiedorn MO, Knoska J, Mazalova V, Roy-Chowdhury S, Yang JH, Jones A, Bean R, Bielecki J, Kim Y, Mills G, Weinhausen B, Meza JD, Al-Qudami N, Bajt S, Brehm G, Botha S, Boukhelef D, Brockhauser S, Bruce BD, Coleman MA, Danilevski C, Discianno E, Dobson Z, Fangohr H, Martin-Garcia JM, Gevorkov Y, Hauf S, Hosseinizadeh A, Januschek F, Ketawala GK, Kupitz C, Maia L, Manetti M, Messerschmidt M, Michelat T, Mondal J, Ourmazd A, Previtali G, Sarrou I, Schön S, Schwander P, Shelby ML, Silenzi A, Sztuk-Dambietz J, Szuba J, Turcato M, White TA, Wrona K, Xu C, Abdellatif MH, Zook JD, Spence JCH, Chapman HN, Barty A, Kirian RA, Frank M, Ros A, Schmidt M, Fromme R, Mancuso AP, Fromme P, and Zatsepin NA
- Abstract
An amendment to this paper has been published and can be accessed via a link at the top of the paper.
- Published
- 2020
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120. Time-resolved serial femtosecond crystallography at the European XFEL.
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Pandey S, Bean R, Sato T, Poudyal I, Bielecki J, Cruz Villarreal J, Yefanov O, Mariani V, White TA, Kupitz C, Hunter M, Abdellatif MH, Bajt S, Bondar V, Echelmeier A, Doppler D, Emons M, Frank M, Fromme R, Gevorkov Y, Giovanetti G, Jiang M, Kim D, Kim Y, Kirkwood H, Klimovskaia A, Knoska J, Koua FHM, Letrun R, Lisova S, Maia L, Mazalova V, Meza D, Michelat T, Ourmazd A, Palmer G, Ramilli M, Schubert R, Schwander P, Silenzi A, Sztuk-Dambietz J, Tolstikova A, Chapman HN, Ros A, Barty A, Fromme P, Mancuso AP, and Schmidt M
- Subjects
- Light, Models, Molecular, Time Factors, Bacterial Proteins chemistry, Crystallography, X-Ray instrumentation, Crystallography, X-Ray methods, Photoreceptors, Microbial chemistry, Protein Conformation
- Abstract
The European XFEL (EuXFEL) is a 3.4-km long X-ray source, which produces femtosecond, ultrabrilliant and spatially coherent X-ray pulses at megahertz (MHz) repetition rates. This X-ray source has been designed to enable the observation of ultrafast processes with near-atomic spatial resolution. Time-resolved crystallographic investigations on biological macromolecules belong to an important class of experiments that explore fundamental and functional structural displacements in these molecules. Due to the unusual MHz X-ray pulse structure at the EuXFEL, these experiments are challenging. Here, we demonstrate how a biological reaction can be followed on ultrafast timescales at the EuXFEL. We investigate the picosecond time range in the photocycle of photoactive yellow protein (PYP) with MHz X-ray pulse rates. We show that difference electron density maps of excellent quality can be obtained. The results connect the previously explored femtosecond PYP dynamics to timescales accessible at synchrotrons. This opens the door to a wide range of time-resolved studies at the EuXFEL.
- Published
- 2020
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121. Membrane protein megahertz crystallography at the European XFEL.
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Gisriel C, Coe J, Letrun R, Yefanov OM, Luna-Chavez C, Stander NE, Lisova S, Mariani V, Kuhn M, Aplin S, Grant TD, Dörner K, Sato T, Echelmeier A, Cruz Villarreal J, Hunter MS, Wiedorn MO, Knoska J, Mazalova V, Roy-Chowdhury S, Yang JH, Jones A, Bean R, Bielecki J, Kim Y, Mills G, Weinhausen B, Meza JD, Al-Qudami N, Bajt S, Brehm G, Botha S, Boukhelef D, Brockhauser S, Bruce BD, Coleman MA, Danilevski C, Discianno E, Dobson Z, Fangohr H, Martin-Garcia JM, Gevorkov Y, Hauf S, Hosseinizadeh A, Januschek F, Ketawala GK, Kupitz C, Maia L, Manetti M, Messerschmidt M, Michelat T, Mondal J, Ourmazd A, Previtali G, Sarrou I, Schön S, Schwander P, Shelby ML, Silenzi A, Sztuk-Dambietz J, Szuba J, Turcato M, White TA, Wrona K, Xu C, Abdellatif MH, Zook JD, Spence JCH, Chapman HN, Barty A, Kirian RA, Frank M, Ros A, Schmidt M, Fromme R, Mancuso AP, Fromme P, and Zatsepin NA
- Subjects
- Crystallography, Cyanobacteria metabolism, Models, Molecular, Photosystem I Protein Complex chemistry, Photosystem I Protein Complex isolation & purification, Static Electricity, Synchrotrons, Thermosynechococcus, X-Rays, Electrons, Lasers, Membrane Proteins chemistry
- Abstract
The world's first superconducting megahertz repetition rate hard X-ray free-electron laser (XFEL), the European XFEL, began operation in 2017, featuring a unique pulse train structure with 886 ns between pulses. With its rapid pulse rate, the European XFEL may alleviate some of the increasing demand for XFEL beamtime, particularly for membrane protein serial femtosecond crystallography (SFX), leveraging orders-of-magnitude faster data collection. Here, we report the first membrane protein megahertz SFX experiment, where we determined a 2.9 Å-resolution SFX structure of the large membrane protein complex, Photosystem I, a > 1 MDa complex containing 36 protein subunits and 381 cofactors. We address challenges to megahertz SFX for membrane protein complexes, including growth of large quantities of crystals and the large molecular and unit cell size that influence data collection and analysis. The results imply that megahertz crystallography could have an important impact on structure determination of large protein complexes with XFELs.
- Published
- 2019
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122. Snapshot of an oxygen intermediate in the catalytic reaction of cytochrome c oxidase.
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Ishigami I, Lewis-Ballester A, Echelmeier A, Brehm G, Zatsepin NA, Grant TD, Coe JD, Lisova S, Nelson G, Zhang S, Dobson ZF, Boutet S, Sierra RG, Batyuk A, Fromme P, Fromme R, Spence JCH, Ros A, Yeh SR, and Rousseau DL
- Subjects
- Animals, Catalysis, Catalytic Domain, Cattle, Copper chemistry, Crystallography, X-Ray, Electron Transport Complex IV genetics, Oxidation-Reduction, Protein Conformation, Electron Transport Complex IV chemistry, Heme chemistry, Iron chemistry, Oxygen chemistry
- Abstract
Cytochrome c oxidase (C c O) reduces dioxygen to water and harnesses the chemical energy to drive proton translocation across the inner mitochondrial membrane by an unresolved mechanism. By using time-resolved serial femtosecond crystallography, we identified a key oxygen intermediate of bovine C c O. It is assigned to the P
R -intermediate, which is characterized by specific redox states of the metal centers and a distinct protein conformation. The heme a3 iron atom is in a ferryl (Fe4+ = O2- ) configuration, and heme a and CuB are oxidized while CuA is reduced. A Helix-X segment is poised in an open conformational state; the heme a farnesyl sidechain is H-bonded to S382, and loop-I-II adopts a distinct structure. These data offer insights into the mechanism by which the oxygen chemistry is coupled to unidirectional proton translocation., Competing Interests: The authors declare no conflict of interest.- Published
- 2019
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123. Free-electron laser data for multiple-particle fluctuation scattering analysis.
- Author
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Pande K, Donatelli JJ, Malmerberg E, Foucar L, Poon BK, Sutter M, Botha S, Basu S, Bruce Doak R, Dörner K, Epp SW, Englert L, Fromme R, Hartmann E, Hartmann R, Hauser G, Hattne J, Hosseinizadeh A, Kassemeyer S, Lomb L, Montero SFC, Menzel A, Rolles D, Rudenko A, Seibert MM, Sierra RG, Schwander P, Ourmazd A, Fromme P, Sauter NK, Bogan M, Bozek J, Bostedt C, Schlichting I, Kerfeld CA, and Zwart PH
- Subjects
- Phycodnaviridae, Scattering, Small Angle, X-Ray Diffraction
- Abstract
Fluctuation X-ray scattering (FXS) is an emerging experimental technique in which solution scattering data are collected using X-ray exposures below rotational diffusion times, resulting in angularly anisotropic X-ray snapshots that provide several orders of magnitude more information than traditional solution scattering data. Such experiments can be performed using the ultrashort X-ray pulses provided by a free-electron laser source, allowing one to collect a large number of diffraction patterns in a relatively short time. Here, we describe a test data set for FXS, obtained at the Linac Coherent Light Source, consisting of close to 100 000 multi-particle diffraction patterns originating from approximately 50 to 200 Paramecium Bursaria Chlorella virus particles per snapshot. In addition to the raw data, a selection of high-quality pre-processed diffraction patterns and a reference SAXS profile are provided.
- Published
- 2018
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124. Enzyme intermediates captured "on the fly" by mix-and-inject serial crystallography.
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Olmos JL Jr, Pandey S, Martin-Garcia JM, Calvey G, Katz A, Knoska J, Kupitz C, Hunter MS, Liang M, Oberthuer D, Yefanov O, Wiedorn M, Heyman M, Holl M, Pande K, Barty A, Miller MD, Stern S, Roy-Chowdhury S, Coe J, Nagaratnam N, Zook J, Verburgt J, Norwood T, Poudyal I, Xu D, Koglin J, Seaberg MH, Zhao Y, Bajt S, Grant T, Mariani V, Nelson G, Subramanian G, Bae E, Fromme R, Fung R, Schwander P, Frank M, White TA, Weierstall U, Zatsepin N, Spence J, Fromme P, Chapman HN, Pollack L, Tremblay L, Ourmazd A, Phillips GN Jr, and Schmidt M
- Subjects
- Bacterial Proteins genetics, Biocatalysis, Cephalosporin Resistance genetics, Kinetics, Lasers, Models, Molecular, Time Factors, beta-Lactamases genetics, Anti-Bacterial Agents chemistry, Bacterial Proteins chemistry, Ceftriaxone chemistry, Crystallography, X-Ray methods, Mycobacterium tuberculosis enzymology, beta-Lactamases chemistry
- Abstract
Background: Ever since the first atomic structure of an enzyme was solved, the discovery of the mechanism and dynamics of reactions catalyzed by biomolecules has been the key goal for the understanding of the molecular processes that drive life on earth. Despite a large number of successful methods for trapping reaction intermediates, the direct observation of an ongoing reaction has been possible only in rare and exceptional cases., Results: Here, we demonstrate a general method for capturing enzyme catalysis "in action" by mix-and-inject serial crystallography (MISC). Specifically, we follow the catalytic reaction of the Mycobacterium tuberculosis β-lactamase with the third-generation antibiotic ceftriaxone by time-resolved serial femtosecond crystallography. The results reveal, in near atomic detail, antibiotic cleavage and inactivation from 30 ms to 2 s., Conclusions: MISC is a versatile and generally applicable method to investigate reactions of biological macromolecules, some of which are of immense biological significance and might be, in addition, important targets for structure-based drug design. With megahertz X-ray pulse rates expected at the Linac Coherent Light Source II and the European X-ray free-electron laser, multiple, finely spaced time delays can be collected rapidly, allowing a comprehensive description of biomolecular reactions in terms of structure and kinetics from the same set of X-ray data.
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- 2018
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125. Corrigendum: Diffraction data of core-shell nanoparticles from an X-ray free electron laser.
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Li X, Chiu CY, Wang HJ, Kassemeyer S, Botha S, Shoeman RL, Lawrence RM, Kupitz C, Kirian R, James D, Wang D, Nelson G, Messerschmidt M, Boutet S, Williams GJ, Hartmann E, Jafarpour A, Foucar LM, Barty A, Chapman H, Liang M, Menzel A, Wang F, Basu S, Fromme R, Doak RB, Fromme P, Weierstall U, Huang MH, Spence JCH, Schlichting I, Hogue BG, and Liu H
- Abstract
This corrects the article DOI: 10.1038/sdata.2017.48.
- Published
- 2017
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126. Femtosecond structural dynamics drives the trans/cis isomerization in photoactive yellow protein.
- Author
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Pande K, Hutchison CD, Groenhof G, Aquila A, Robinson JS, Tenboer J, Basu S, Boutet S, DePonte DP, Liang M, White TA, Zatsepin NA, Yefanov O, Morozov D, Oberthuer D, Gati C, Subramanian G, James D, Zhao Y, Koralek J, Brayshaw J, Kupitz C, Conrad C, Roy-Chowdhury S, Coe JD, Metz M, Xavier PL, Grant TD, Koglin JE, Ketawala G, Fromme R, Šrajer V, Henning R, Spence JC, Ourmazd A, Schwander P, Weierstall U, Frank M, Fromme P, Barty A, Chapman HN, Moffat K, van Thor JJ, and Schmidt M
- Subjects
- Crystallography, Isomerism, Light, Photons, Protein Conformation radiation effects, Time Factors, Bacterial Proteins chemistry, Bacterial Proteins radiation effects, Photochemical Processes, Photoreceptors, Microbial chemistry, Photoreceptors, Microbial radiation effects
- Abstract
A variety of organisms have evolved mechanisms to detect and respond to light, in which the response is mediated by protein structural changes after photon absorption. The initial step is often the photoisomerization of a conjugated chromophore. Isomerization occurs on ultrafast time scales and is substantially influenced by the chromophore environment. Here we identify structural changes associated with the earliest steps in the trans-to-cis isomerization of the chromophore in photoactive yellow protein. Femtosecond hard x-ray pulses emitted by the Linac Coherent Light Source were used to conduct time-resolved serial femtosecond crystallography on photoactive yellow protein microcrystals over a time range from 100 femtoseconds to 3 picoseconds to determine the structural dynamics of the photoisomerization reaction., (Copyright © 2016, American Association for the Advancement of Science.)
- Published
- 2016
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127. Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser.
- Author
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Kang Y, Zhou XE, Gao X, He Y, Liu W, Ishchenko A, Barty A, White TA, Yefanov O, Han GW, Xu Q, de Waal PW, Ke J, Tan MH, Zhang C, Moeller A, West GM, Pascal BD, Van Eps N, Caro LN, Vishnivetskiy SA, Lee RJ, Suino-Powell KM, Gu X, Pal K, Ma J, Zhi X, Boutet S, Williams GJ, Messerschmidt M, Gati C, Zatsepin NA, Wang D, James D, Basu S, Roy-Chowdhury S, Conrad CE, Coe J, Liu H, Lisova S, Kupitz C, Grotjohann I, Fromme R, Jiang Y, Tan M, Yang H, Li J, Wang M, Zheng Z, Li D, Howe N, Zhao Y, Standfuss J, Diederichs K, Dong Y, Potter CS, Carragher B, Caffrey M, Jiang H, Chapman HN, Spence JC, Fromme P, Weierstall U, Ernst OP, Katritch V, Gurevich VV, Griffin PR, Hubbell WL, Stevens RC, Cherezov V, Melcher K, and Xu HE
- Subjects
- Animals, Binding Sites, Crystallography, X-Ray, Disulfides chemistry, Disulfides metabolism, Humans, Lasers, Mice, Models, Molecular, Multiprotein Complexes biosynthesis, Multiprotein Complexes chemistry, Multiprotein Complexes metabolism, Protein Binding, Reproducibility of Results, Signal Transduction, X-Rays, Arrestin chemistry, Arrestin metabolism, Rhodopsin chemistry, Rhodopsin metabolism
- Abstract
G-protein-coupled receptors (GPCRs) signal primarily through G proteins or arrestins. Arrestin binding to GPCRs blocks G protein interaction and redirects signalling to numerous G-protein-independent pathways. Here we report the crystal structure of a constitutively active form of human rhodopsin bound to a pre-activated form of the mouse visual arrestin, determined by serial femtosecond X-ray laser crystallography. Together with extensive biochemical and mutagenesis data, the structure reveals an overall architecture of the rhodopsin-arrestin assembly in which rhodopsin uses distinct structural elements, including transmembrane helix 7 and helix 8, to recruit arrestin. Correspondingly, arrestin adopts the pre-activated conformation, with a ∼20° rotation between the amino and carboxy domains, which opens up a cleft in arrestin to accommodate a short helix formed by the second intracellular loop of rhodopsin. This structure provides a basis for understanding GPCR-mediated arrestin-biased signalling and demonstrates the power of X-ray lasers for advancing the frontiers of structural biology.
- Published
- 2015
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128. Crystallization of Photosystem II for Time-Resolved Structural Studies Using an X-ray Free Electron Laser.
- Author
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Coe J, Kupitz C, Basu S, Conrad CE, Roy-Chowdhury S, Fromme R, and Fromme P
- Subjects
- Crystallization instrumentation, Crystallization methods, Crystallography, X-Ray instrumentation, Electrons, Equipment Design, Lasers, Models, Molecular, Photosystem II Protein Complex isolation & purification, Protein Conformation, Crystallography, X-Ray methods, Photosystem II Protein Complex chemistry, Synechococcus chemistry
- Abstract
Photosystem II (PSII) is a membrane protein supercomplex that executes the initial reaction of photosynthesis in higher plants, algae, and cyanobacteria. It captures the light from the sun to catalyze a transmembrane charge separation. In a series of four charge separation events, utilizing the energy from four photons, PSII oxidizes two water molecules to obtain dioxygen, four protons, and four electrons. The light reactions of photosystems I and II (PSI and PSII) result in the formation of an electrochemical transmembrane proton gradient that is used for the production of ATP. Electrons that are subsequently transferred from PSI via the soluble protein ferredoxin to ferredoxin-NADP(+) reductase that reduces NADP(+) to NADPH. The products of photosynthesis and the elemental oxygen evolved sustain all higher life on Earth. All oxygen in the atmosphere is produced by the oxygen-evolving complex in PSII, a process that changed our planet from an anoxygenic to an oxygenic atmosphere 2.5 billion years ago. In this chapter, we provide recent insight into the mechanisms of this process and methods used in probing this question., (© 2015 Elsevier Inc. All rights reserved.)
- Published
- 2015
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129. Microcrystallization techniques for serial femtosecond crystallography using photosystem II from Thermosynechococcus elongatus as a model system.
- Author
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Kupitz C, Grotjohann I, Conrad CE, Roy-Chowdhury S, Fromme R, and Fromme P
- Subjects
- Cyanobacteria, Nanoparticles chemistry, Protein Conformation, Crystallization methods, Crystallography, X-Ray methods, Electrons, Lasers, Photosystem II Protein Complex chemistry, X-Ray Diffraction methods
- Abstract
Serial femtosecond crystallography (SFX) is a new emerging method, where X-ray diffraction data are collected from a fully hydrated stream of nano- or microcrystals of biomolecules in their mother liquor using high-energy, X-ray free-electron lasers. The success of SFX experiments strongly depends on the ability to grow large amounts of well-ordered nano/microcrystals of homogeneous size distribution. While methods to grow large single crystals have been extensively explored in the past, method developments to grow nano/microcrystals in sufficient amounts for SFX experiments are still in their infancy. Here, we describe and compare three methods (batch, free interface diffusion (FID) and FID centrifugation) for growth of nano/microcrystals for time-resolved SFX experiments using the large membrane protein complex photosystem II as a model system., (© 2014 The Author(s) Published by the Royal Society. All rights reserved.)
- Published
- 2014
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130. Time-resolved protein nanocrystallography using an X-ray free-electron laser.
- Author
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Aquila A, Hunter MS, Doak RB, Kirian RA, Fromme P, White TA, Andreasson J, Arnlund D, Bajt S, Barends TR, Barthelmess M, Bogan MJ, Bostedt C, Bottin H, Bozek JD, Caleman C, Coppola N, Davidsson J, DePonte DP, Elser V, Epp SW, Erk B, Fleckenstein H, Foucar L, Frank M, Fromme R, Graafsma H, Grotjohann I, Gumprecht L, Hajdu J, Hampton CY, Hartmann A, Hartmann R, Hau-Riege S, Hauser G, Hirsemann H, Holl P, Holton JM, Hömke A, Johansson L, Kimmel N, Kassemeyer S, Krasniqi F, Kühnel KU, Liang M, Lomb L, Malmerberg E, Marchesini S, Martin AV, Maia FR, Messerschmidt M, Nass K, Reich C, Neutze R, Rolles D, Rudek B, Rudenko A, Schlichting I, Schmidt C, Schmidt KE, Schulz J, Seibert MM, Shoeman RL, Sierra R, Soltau H, Starodub D, Stellato F, Stern S, Strüder L, Timneanu N, Ullrich J, Wang X, Williams GJ, Weidenspointner G, Weierstall U, Wunderer C, Barty A, Spence JC, and Chapman HN
- Subjects
- Electrons, Protein Conformation, X-Rays, Crystallography, X-Ray methods, Ferredoxins ultrastructure, Lasers, Nanostructures ultrastructure, X-Ray Diffraction methods
- Abstract
We demonstrate the use of an X-ray free electron laser synchronized with an optical pump laser to obtain X-ray diffraction snapshots from the photoactivated states of large membrane protein complexes in the form of nanocrystals flowing in a liquid jet. Light-induced changes of Photosystem I-Ferredoxin co-crystals were observed at time delays of 5 to 10 µs after excitation. The result correlates with the microsecond kinetics of electron transfer from Photosystem I to ferredoxin. The undocking process that follows the electron transfer leads to large rearrangements in the crystals that will terminally lead to the disintegration of the crystals. We describe the experimental setup and obtain the first time-resolved femtosecond serial X-ray crystallography results from an irreversible photo-chemical reaction at the Linac Coherent Light Source. This technique opens the door to time-resolved structural studies of reaction dynamics in biological systems.
- Published
- 2012
- Full Text
- View/download PDF
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