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. HunterStephan Kassemeyer, Richard 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 Zatsepin, Sébastien Boutet, John Spence, Ilme Schlichting, Henry N. Chapman, Petra Fromme, Richard Neutze

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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.

Original languageEnglish (US)
Article number2911
JournalNature communications
Volume4
DOIs
StatePublished - Dec 19 2013

ASJC Scopus subject areas

  • General Chemistry
  • General Biochemistry, Genetics and Molecular Biology
  • General Physics and Astronomy

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  • Serial femtosecond crystallography structure of a photosynthetic reaction center

    Johansson, L. C. (Contributor), Arnlund, D. (Contributor), Katona, G. (Contributor), White, T. A. (Contributor), Barty, A. (Contributor), Deponte, D. P. (Contributor), Shoeman, R. L. (Contributor), Wickstrand, C. (Contributor), Sharma, A. (Contributor), Williams, G. J. (Contributor), Aquila, A. (Contributor), Bogan, M. J. (Contributor), Caleman, C. (Contributor), Davidsson, J. (Contributor), Doak, R. B. (Contributor), Frank, M. (Contributor), Fromme, R. (Contributor), Galli, L. (Contributor), Grotjohann, I. (Contributor), Hunter, M. S. (Contributor), Kassemeyer, S. (Contributor), Kirian, R. (Contributor), Kupitz, C. (Contributor), Liang, M. (Contributor), Lomb, L. (Contributor), Malmerberg, E. (Contributor), Martin, A. V. (Contributor), Messerschmidt, M. (Contributor), Nass, K. (Contributor), Redecke, L. (Contributor), Seibert, M. M. (Contributor), Sjöhamn, J. (Contributor), Steinbrener, J. (Contributor), Stellato, F. (Contributor), Wang, D. (Contributor), Wahlgren, W. Y. (Contributor), Weierstall, U. (Contributor), Westenhoff, S. (Contributor), Zatsepin, N. A. (Contributor), Boutet, S. (Contributor), Spence, J. C. H. (Contributor), Schlichting, I. (Contributor), Chapman, H. N. (Contributor), Fromme, P. (Contributor) & Neutze, R. (Contributor), Protein Data Bank (PDB), Dec 25 2013

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