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Journal Article

Structure of a photosynthetic reaction centre determined by serial femtosecond crystallography

MPS-Authors
http://pubman.mpdl.mpg.de/cone/persons/resource/persons95345

Shoeman,  Robert L.
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons93693

Kassemeyer,  Stephan
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons94117

Lomb,  Lukas
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons117908

Steinbrener,  Jan
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons95189

Schlichting,  Ilme
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Johansson, L. C., Arnlund, D., Katona, G., White, T. A., Barty, A., DePonte, D. P., et al. (2013). Structure of a photosynthetic reaction centre determined by serial femtosecond crystallography. Nature Communications, 4: 2911, pp. 1-7. doi:10.1038/ncomms3911.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-98AF-D
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.