Journal Article

PUBDB-2017-11676

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Pink-beam serial crystallography

Meents, A. (Corresponding author)CFEL*DESY* ; Wiedorn, M. O.CFEL*DESY* ; Srajer, V. ; Henning, R. ; Sarrou, I.CFEL* ; Bergtholdt, J.CFEL* ; Barthelmess, M.CFEL* ; Reinke, P. Y. A. ; Dierksmeyer, D.CFEL* ; Tolstikova, A.CFEL* ; Schaible, S.Extern* ; Messerschmidt, M.XFEL.EU* ; Ogata, C. M. ; Kissick, D. J. ; Taft, M. H. ; Manstein, D. J. ; Lieske, J.DESY* ; Oberthür, D.CFEL*DESY* ; Fischetti, R. F. ; Chapman, H. N.CFEL*DESY*

2017
Nature Publishing Group London

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Please use a persistent id in citations: doi:10.1038/s41467-017-01417-3  doi:10.3204/PUBDB-2017-11676

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.

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Contributing Institute(s):

1. FS-CFEL-1 (Group Leader: Henry Chapman) (CFEL-I)
2. FS-Photon Science (FS-PS)

Research Program(s):

1. 6215 - Soft Matter, Health and Life Sciences (POF3-621) (POF3-621)
2. X-probe - Advanced XFEL and Synchrotron based Probes of Protein Structure and Dynamics (637295) (637295)
3. BMBF-05K14CHA - 05K14CHA - SyncFELmed: Teilprojekt 2 (BMBF-05K14CHA) (BMBF-05K14CHA)
4. VH-VI-419 - Dynamic Pathways in Multidimensional Landscapes (VH-VI-419) (VH-VI-419)
5. VH-VI-403 - In-Situ Nano-Imaging of Biological and Chemical Processes (2015_IFV-VH-VI-403) (2015_IFV-VH-VI-403)
6. EUCALL - European Cluster of Advanced Laser Light Sources (654220) (654220)

Experiment(s):

1. Experiments at CFEL
2. Measurement at external facility

Appears in the scientific report 2017

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Database coverage:
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