Pink-beam serial crystallography

A. Meents (), M. O. Wiedorn, V. Srajer, R. Henning, I. Sarrou, J. Bergtholdt, M. Barthelmess, P. Y. A. Reinke, D. Dierksmeyer, A. Tolstikova, S. Schaible, M. Messerschmidt, C. M. Ogata, D. J. Kissick, M. H. Taft, D. J. Manstein, J. Lieske, D. Oberthuer, R. F. Fischetti and H. N. Chapman
Additional contact information
A. Meents: Center for Free Electron Laser Science, DESY
M. O. Wiedorn: Center for Free Electron Laser Science, DESY
V. Srajer: Center for Advanced Radiation Sources, The University of Chicago
R. Henning: Center for Advanced Radiation Sources, The University of Chicago
I. Sarrou: Center for Free Electron Laser Science, DESY
J. Bergtholdt: Center for Free Electron Laser Science, DESY
M. Barthelmess: Center for Free Electron Laser Science, DESY
P. Y. A. Reinke: Medizinische Hochschule Hannover (MHH), Institut für Biophysikalische Chemie
D. Dierksmeyer: Center for Free Electron Laser Science, DESY
A. Tolstikova: University of Hamburg
S. Schaible: Deutsches Elektronen Synchrotron (DESY), Photon Science
M. Messerschmidt: National Science Foundation BioXFEL Science and Technology Center
C. M. Ogata: Advanced Photon Source, Argonne National Laboratory
D. J. Kissick: Advanced Photon Source, Argonne National Laboratory
M. H. Taft: Medizinische Hochschule Hannover (MHH), Institut für Biophysikalische Chemie
D. J. Manstein: Medizinische Hochschule Hannover (MHH), Institut für Biophysikalische Chemie
J. Lieske: Deutsches Elektronen Synchrotron (DESY), Photon Science
D. Oberthuer: Center for Free Electron Laser Science, DESY
R. F. Fischetti: Advanced Photon Source, Argonne National Laboratory
H. N. Chapman: Center for Free Electron Laser Science, DESY

Nature Communications, 2017, vol. 8, issue 1, 1-12

Abstract: Abstract Serial X-ray crystallography allows macromolecular structure determination at both X-ray free electron lasers (XFELs) and, more recently, synchrotron sources. The time resolution for serial synchrotron crystallography experiments has been limited to millisecond timescales with monochromatic beams. The polychromatic, “pink”, beam provides a more than two orders of magnitude increased photon flux and hence allows accessing much shorter timescales in diffraction experiments at synchrotron sources. Here we report the structure determination of two different protein samples by merging pink-beam diffraction patterns from many crystals, each collected with a single 100 ps X-ray pulse exposure per crystal using a setup optimized for very low scattering background. In contrast to experiments with monochromatic radiation, data from only 50 crystals were required to obtain complete datasets. The high quality of the diffraction data highlights the potential of this method for studying irreversible reactions at sub-microsecond timescales using high-brightness X-ray facilities.

Date: 2017
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DOI: 10.1038/s41467-017-01417-3

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