Journal article

Lipidic cubic phase serial millisecond crystallography using synchrotron radiation.

  • Nogly P Laboratory for Biomolecular Research, Paul Scherrer Institute, Villigen 5232, Switzerland.
  • James D Department of Physics, Arizona State University, Tempe, AZ 85287, USA.
  • Wang D Department of Physics, Arizona State University, Tempe, AZ 85287, USA.
  • White TA Center for Free-Electron Laser Science, Deutsches Elektronen-Synchrotron DESY, Hamburg 22607, Germany.
  • Zatsepin N Department of Physics, Arizona State University, Tempe, AZ 85287, USA.
  • Shilova A European Synchrotron Radiation Facility, Grenoble Cedex 9, F-38043, France.
  • Nelson G Department of Physics, Arizona State University, Tempe, AZ 85287, USA.
  • Liu H Department of Physics, Arizona State University, Tempe, AZ 85287, USA.
  • Johansson L Department of Integrative Structural and Computational Biology, Scripps Research Institute, La Jolla, California USA.
  • Heymann M Center for Free-Electron Laser Science, Deutsches Elektronen-Synchrotron DESY, Hamburg 22607, Germany.
  • Jaeger K Laboratory for Biomolecular Research, Paul Scherrer Institute, Villigen 5232, Switzerland.
  • Metz M Center for Free-Electron Laser Science, Deutsches Elektronen-Synchrotron DESY, Hamburg 22607, Germany ; Centre for Ultrafast Imaging, Hamburg 22607, Germany.
  • Wickstrand C Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.
  • Wu W Laboratory for Biomolecular Research, Paul Scherrer Institute, Villigen 5232, Switzerland.
  • Båth P Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.
  • Berntsen P Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.
  • Oberthuer D Center for Free-Electron Laser Science, Deutsches Elektronen-Synchrotron DESY, Hamburg 22607, Germany ; Centre for Ultrafast Imaging, Hamburg 22607, Germany.
  • Panneels V Laboratory for Biomolecular Research, Paul Scherrer Institute, Villigen 5232, Switzerland.
  • Cherezov V Department of Integrative Structural and Computational Biology, Scripps Research Institute, La Jolla, California USA.
  • Chapman H Center for Free-Electron Laser Science, Deutsches Elektronen-Synchrotron DESY, Hamburg 22607, Germany ; Department of Physics, University of Hamburg, Hamburg 22607, Germany.
  • Schertler G Laboratory for Biomolecular Research, Paul Scherrer Institute, Villigen 5232, Switzerland ; Deparment of Biology, ETH Zurich, Zürich 8093, Switzerland.
  • Neutze R Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.
  • Spence J Department of Physics, Arizona State University, Tempe, AZ 85287, USA.
  • Moraes I Membrane Protein Laboratory, Diamond Light Source, Harwell Science and Innovation Campus, Chilton, Oxfordshire OX11 0DE, England ; Department of Life Sciences, Imperial College London, London, England ; Research Complex at Harwell Rutherford, Appleton Laboratory, Harwell, Didcot, Oxfordshire OX11 0FA, England.
  • Burghammer M European Synchrotron Radiation Facility, Grenoble Cedex 9, F-38043, France ; Department of Analytical Chemistry, Ghent University, Ghent B-9000, Belgium.
  • Standfuss J Laboratory for Biomolecular Research, Paul Scherrer Institute, Villigen 5232, Switzerland.
  • Weierstall U Department of Physics, Arizona State University, Tempe, AZ 85287, USA.
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  • 2015-04-14
Published in:
  • IUCrJ. - 2015
English Lipidic cubic phases (LCPs) have emerged as successful matrixes for the crystallization of membrane proteins. Moreover, the viscous LCP also provides a highly effective delivery medium for serial femtosecond crystallography (SFX) at X-ray free-electron lasers (XFELs). Here, the adaptation of this technology to perform serial millisecond crystallography (SMX) at more widely available synchrotron microfocus beamlines is described. Compared with conventional microcrystallography, LCP-SMX eliminates the need for difficult handling of individual crystals and allows for data collection at room temperature. The technology is demonstrated by solving a structure of the light-driven proton-pump bacteriorhodopsin (bR) at a resolution of 2.4 Å. The room-temperature structure of bR is very similar to previous cryogenic structures but shows small yet distinct differences in the retinal ligand and proton-transfer pathway.
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  • English
Open access status
gold
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https://sonar.ch/global/documents/136735
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