Structure of a photosynthetic reaction centre determined by serial femtosecond crystallography

Linda C. Johansson, David Arnlund, Gergely Katona, Thomas A. White, Anton Barty, Daniel P. DePonte, Robert L. Shoeman, Cecilia Wickstrand, Amit Sharma, Garth J. Williams, Andrew Aquila, Michael J. Bogan, Carl Caleman, Jan Davidsson, R Bruce Doak, Matthias Frank, Raimund Fromme, Lorenzo Galli, Ingo Grotjohann, Mark S. Hunter, Stephan Kassemeyer, Richard A. Kirian, Christopher Kupitz, Mengning Liang, Lukas Lomb, Erik Malmerberg, Andrew V. Martin, Marc Messerschmidt, Karol Nass, Lars Redecke, M Marvin Seibert, Jennie Sjöhamn, Jan Steinbrener, Francesco Stellato, Dingjie Wang, Weixaio Y. Wahlgren, Uwe Weierstall, Sebastian Westenhoff, Nadia A. Zatsepin, Sébastien Boutet, John C.H. Spence, Ilme Schlichting, Henry N. Chapman, Petra Fromme and Richard Neutze ()
Additional contact information
Linda C. Johansson: University of Gothenburg
David Arnlund: University of Gothenburg
Gergely Katona: University of Gothenburg
Thomas A. White: Center for Free-Electron Laser Science, DESY
Anton Barty: Center for Free-Electron Laser Science, DESY
Daniel P. DePonte: Center for Free-Electron Laser Science, DESY
Robert L. Shoeman: Max-Planck-Institut für Medizinische Forschung
Cecilia Wickstrand: University of Gothenburg
Amit Sharma: University of Gothenburg
Garth J. Williams: Linac Coherent Light Source, LCLS, SLAC National Accelerator Laboratory
Andrew Aquila: Center for Free-Electron Laser Science, DESY
Michael J. Bogan: PULSE Institute, SLAC National Accelerator Laboratory
Carl Caleman: Center for Free-Electron Laser Science, DESY
Jan Davidsson: Uppsala University
R Bruce Doak: Arizona State University
Matthias Frank: Lawrence Livermore National Laboratory
Raimund Fromme: Arizona State University
Lorenzo Galli: Center for Free-Electron Laser Science, DESY
Ingo Grotjohann: Arizona State University
Mark S. Hunter: Arizona State University
Stephan Kassemeyer: Max-Planck-Institut für Medizinische Forschung
Richard A. Kirian: Arizona State University
Christopher Kupitz: Arizona State University
Mengning Liang: Center for Free-Electron Laser Science, DESY
Lukas Lomb: Max-Planck-Institut für Medizinische Forschung
Erik Malmerberg: University of Gothenburg
Andrew V. Martin: Center for Free-Electron Laser Science, DESY
Marc Messerschmidt: Linac Coherent Light Source, LCLS, SLAC National Accelerator Laboratory
Karol Nass: Center for Free-Electron Laser Science, DESY
Lars Redecke: Joint Laboratory for Structural Biology of Infection and Inflammation, Institute of Biochemistry and Molecular Biology, University of Hamburg and Institute of Biochemistry, University of Lübeck at DESY
M Marvin Seibert: Linac Coherent Light Source, LCLS, SLAC National Accelerator Laboratory
Jennie Sjöhamn: University of Gothenburg
Jan Steinbrener: Max-Planck-Institut für Medizinische Forschung
Francesco Stellato: Center for Free-Electron Laser Science, DESY
Dingjie Wang: Arizona State University
Weixaio Y. Wahlgren: University of Gothenburg
Uwe Weierstall: Arizona State University
Sebastian Westenhoff: University of Gothenburg
Nadia A. Zatsepin: Arizona State University
Sébastien Boutet: Linac Coherent Light Source, LCLS, SLAC National Accelerator Laboratory
John C.H. Spence: Arizona State University
Ilme Schlichting: Max-Planck-Institut für Medizinische Forschung
Henry N. Chapman: Center for Free-Electron Laser Science, DESY
Petra Fromme: Arizona State University
Richard Neutze: University of Gothenburg

Nature Communications, 2013, vol. 4, issue 1, 1-7

Abstract: Abstract Serial femtosecond crystallography is an X-ray free-electron-laser-based method with considerable potential to have an impact on challenging problems in structural biology. Here we present X-ray diffraction data recorded from microcrystals of the Blastochloris viridis photosynthetic reaction centre to 2.8 Å resolution and determine its serial femtosecond crystallography structure to 3.5 Å resolution. Although every microcrystal is exposed to a dose of 33 MGy, no signs of X-ray-induced radiation damage are visible in this integral membrane protein structure.

Date: 2013
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DOI: 10.1038/ncomms3911

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