De novo protein crystal structure determination from X-ray free-electron laser data

Thomas R. M. Barends (), Lutz Foucar, Sabine Botha, R. Bruce Doak, Robert L. Shoeman, Karol Nass, Jason E. Koglin, Garth J. Williams, Sébastien Boutet, Marc Messerschmidt and Ilme Schlichting ()
Additional contact information
Thomas R. M. Barends: Max-Planck Institute for Medical Research, Jahnstrasse 29, D-69120 Heidelberg, Germany
Lutz Foucar: Max-Planck Institute for Medical Research, Jahnstrasse 29, D-69120 Heidelberg, Germany
Sabine Botha: Max-Planck Institute for Medical Research, Jahnstrasse 29, D-69120 Heidelberg, Germany
R. Bruce Doak: Max-Planck Institute for Medical Research, Jahnstrasse 29, D-69120 Heidelberg, Germany
Robert L. Shoeman: Max-Planck Institute for Medical Research, Jahnstrasse 29, D-69120 Heidelberg, Germany
Karol Nass: Max-Planck Institute for Medical Research, Jahnstrasse 29, D-69120 Heidelberg, Germany
Jason E. Koglin: SLAC National Accelerator Laboratory, 2575 Sand Hill Road
Garth J. Williams: SLAC National Accelerator Laboratory, 2575 Sand Hill Road
Sébastien Boutet: SLAC National Accelerator Laboratory, 2575 Sand Hill Road
Marc Messerschmidt: SLAC National Accelerator Laboratory, 2575 Sand Hill Road
Ilme Schlichting: Max-Planck Institute for Medical Research, Jahnstrasse 29, D-69120 Heidelberg, Germany

Nature, 2014, vol. 505, issue 7482, 244-247

Abstract: Femtosecond crystallography with an X-ray free-electron laser is used to analyse micrometre-sized protein crystals, generating a high-resolution structure of the protein without previous knowledge of what it looks like.

Date: 2014
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DOI: 10.1038/nature12773

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