Lipidic cubic phase serial millisecond crystallography using synchrotron radiation.
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Nogly P
Laboratory for Biomolecular Research, Paul Scherrer Institute, Villigen 5232, Switzerland.
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James D
Department of Physics, Arizona State University, Tempe, AZ 85287, USA.
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Wang D
Department of Physics, Arizona State University, Tempe, AZ 85287, USA.
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White TA
Center for Free-Electron Laser Science, Deutsches Elektronen-Synchrotron DESY, Hamburg 22607, Germany.
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Zatsepin N
Department of Physics, Arizona State University, Tempe, AZ 85287, USA.
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Shilova A
European Synchrotron Radiation Facility, Grenoble Cedex 9, F-38043, France.
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Nelson G
Department of Physics, Arizona State University, Tempe, AZ 85287, USA.
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Liu H
Department of Physics, Arizona State University, Tempe, AZ 85287, USA.
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Johansson L
Department of Integrative Structural and Computational Biology, Scripps Research Institute, La Jolla, California USA.
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Heymann M
Center for Free-Electron Laser Science, Deutsches Elektronen-Synchrotron DESY, Hamburg 22607, Germany.
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Jaeger K
Laboratory for Biomolecular Research, Paul Scherrer Institute, Villigen 5232, Switzerland.
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Metz M
Center for Free-Electron Laser Science, Deutsches Elektronen-Synchrotron DESY, Hamburg 22607, Germany ; Centre for Ultrafast Imaging, Hamburg 22607, Germany.
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Wickstrand C
Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.
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Wu W
Laboratory for Biomolecular Research, Paul Scherrer Institute, Villigen 5232, Switzerland.
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Båth P
Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.
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Berntsen P
Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.
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Oberthuer D
Center for Free-Electron Laser Science, Deutsches Elektronen-Synchrotron DESY, Hamburg 22607, Germany ; Centre for Ultrafast Imaging, Hamburg 22607, Germany.
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Panneels V
Laboratory for Biomolecular Research, Paul Scherrer Institute, Villigen 5232, Switzerland.
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Cherezov V
Department of Integrative Structural and Computational Biology, Scripps Research Institute, La Jolla, California USA.
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Chapman H
Center for Free-Electron Laser Science, Deutsches Elektronen-Synchrotron DESY, Hamburg 22607, Germany ; Department of Physics, University of Hamburg, Hamburg 22607, Germany.
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Schertler G
Laboratory for Biomolecular Research, Paul Scherrer Institute, Villigen 5232, Switzerland ; Deparment of Biology, ETH Zurich, Zürich 8093, Switzerland.
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Neutze R
Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.
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Spence J
Department of Physics, Arizona State University, Tempe, AZ 85287, USA.
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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.
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Burghammer M
European Synchrotron Radiation Facility, Grenoble Cedex 9, F-38043, France ; Department of Analytical Chemistry, Ghent University, Ghent B-9000, Belgium.
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Standfuss J
Laboratory for Biomolecular Research, Paul Scherrer Institute, Villigen 5232, Switzerland.
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Weierstall U
Department of Physics, Arizona State University, Tempe, AZ 85287, USA.
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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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Language
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Open access status
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gold
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Persistent URL
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https://sonar.ch/global/documents/136735
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