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Title: Pink-beam serial crystallography

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.
Authors:
ORCiD logo [1] ; ORCiD logo [2] ;  [3] ;  [4] ;  [5] ;  [5] ;  [5] ;  [6] ;  [5] ;  [7] ;  [8] ;  [9] ;  [10] ;  [10] ; ORCiD logo [6] ;  [6] ;  [8] ;  [5] ; ORCiD logo [10] ; ORCiD logo [11]
  1. DESY, Hamburg (Germany). Center for Free Electron Laser Science and Photon Science
  2. DESY, Hamburg (Germany). Center for Free Electron Laser Science; University of Hamburg (Germany). Dept. of Physics
  3. Univ. of Chicago, IL (United States). Center for Advanced Radiation Sources
  4. Center for Advanced Radiation Sources
  5. DESY, Hamburg (Germany). Center for Free Electron Laser Science
  6. Institut für Biophysikalische Chemie, Hannover (Germany). Medizinische Hochschule Hannover (MHH)
  7. University of Hamburg (Germany). Dept. of Physics
  8. Deutsches Elektronen Synchrotron (DESY), Hamburg (Germany). Photon Science
  9. National Science Foundation BioXFEL Science and Technology Center, Buffalo, NY (United States)
  10. Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
  11. DESY, Hamburg (Germany). Center for Free Electron Laser Science; University of Hamburg (Germany). Dept. of Physics; Centre for Ultrafast Imaging, Hamburg (Germany)
Publication Date:
Grant/Contract Number:
AC02-06CH11357
Type:
Accepted Manuscript
Journal Name:
Nature Communications
Additional Journal Information:
Journal Volume: 8; Journal Issue: 1; Journal ID: ISSN 2041-1723
Publisher:
Nature Publishing Group
Research Org:
Argonne National Lab. (ANL), Argonne, IL (United States)
Sponsoring Org:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22). Scientific User Facilities Division; European Union - Horizon 2020 Research and Innovation Programme; Helmholtz Association of German Research Centres - Virtual Institute; National Institutes of Health (NIH) - National Institute of General Medical Sciences
Country of Publication:
United States
Language:
English
Subject:
71 CLASSICAL AND QUANTUM MECHANICS, GENERAL PHYSICS; 46 INSTRUMENTATION RELATED TO NUCLEAR SCIENCE AND TECHNOLOGY; Techniques and instrumentation; X-ray crystallography
OSTI Identifier:
1422407

Meents, A., Wiedorn, M. O., Srajer, V., Henning, R., Sarrou, I., Bergtholdt, J., Barthelmess, M., Reinke, P. Y. A., Dierksmeyer, D., Tolstikova, A., Schaible, S., Messerschmidt, M., Ogata, C. M., Kissick, D. J., Taft, M. H., Manstein, D. J., Lieske, J., Oberthuer, D., Fischetti, R. F., and Chapman, H. N.. Pink-beam serial crystallography. United States: N. p., Web. doi:10.1038/s41467-017-01417-3.
Meents, A., Wiedorn, M. O., Srajer, V., Henning, R., Sarrou, I., Bergtholdt, J., Barthelmess, M., Reinke, P. Y. A., Dierksmeyer, D., Tolstikova, A., Schaible, S., Messerschmidt, M., Ogata, C. M., Kissick, D. J., Taft, M. H., Manstein, D. J., Lieske, J., Oberthuer, D., Fischetti, R. F., & Chapman, H. N.. Pink-beam serial crystallography. United States. doi:10.1038/s41467-017-01417-3.
Meents, A., Wiedorn, M. O., Srajer, V., Henning, R., Sarrou, I., Bergtholdt, J., Barthelmess, M., Reinke, P. Y. A., Dierksmeyer, D., Tolstikova, A., Schaible, S., Messerschmidt, M., Ogata, C. M., Kissick, D. J., Taft, M. H., Manstein, D. J., Lieske, J., Oberthuer, D., Fischetti, R. F., and Chapman, H. N.. 2017. "Pink-beam serial crystallography". United States. doi:10.1038/s41467-017-01417-3. https://www.osti.gov/servlets/purl/1422407.
@article{osti_1422407,
title = {Pink-beam serial crystallography},
author = {Meents, A. and Wiedorn, M. O. and Srajer, V. and Henning, R. and Sarrou, I. and Bergtholdt, J. and Barthelmess, M. and Reinke, P. Y. A. and Dierksmeyer, D. and Tolstikova, A. and Schaible, S. and Messerschmidt, M. and Ogata, C. M. and Kissick, D. J. and Taft, M. H. and Manstein, D. J. and Lieske, J. and Oberthuer, D. and Fischetti, R. F. and Chapman, H. N.},
abstractNote = {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.},
doi = {10.1038/s41467-017-01417-3},
journal = {Nature Communications},
number = 1,
volume = 8,
place = {United States},
year = {2017},
month = {11}
}

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Serial femtosecond crystallography of soluble proteins in lipidic cubic phase
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