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IUCrJ. 2019 Apr 5;6(Pt 3):412-425. doi: 10.1107/S205225251900263X. eCollection 2019 May 1.

High-viscosity injector-based pink-beam serial crystallography of microcrystals at a synchrotron radiation source.

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Biodesign Center for Applied Structural Discovery, Biodesign Institute, Arizona State University, 727 East Tyler Street, Tempe, AZ 85287, USA.
School of Molecular Sciences, Arizona State University, 551 East University Drive, Tempe, AZ 85287, USA.
Department of Physics, Arizona State University, 550 East Tyler Drive, Tempe, AZ 85287, USA.
Advanced Photon Source, Argonne National Laboratory, 9700 South Cass Ave, Lemont, IL 90439, USA.
Center for Advanced Radiation Sources, The University of Chicago, Argonne National Laboratory, 9700 South Cass Ave, Lemont, IL 90439, USA.
Department of Chemistry, Bridge Institute, University of Southern California, 1002 Childs Way, Los Angeles, CA 90089, USA.


Since the first successful serial crystallography (SX) experiment at a synchrotron radiation source, the popularity of this approach has continued to grow showing that third-generation synchrotrons can be viable alternatives to scarce X-ray free-electron laser sources. Synchrotron radiation flux may be increased ∼100 times by a moderate increase in the bandwidth ('pink beam' conditions) at some cost to data analysis complexity. Here, we report the first high-viscosity injector-based pink-beam SX experiments. The structures of proteinase K (PK) and A2A adenosine receptor (A2AAR) were determined to resolutions of 1.8 and 4.2 Å using 4 and 24 consecutive 100 ps X-ray pulse exposures, respectively. Strong PK data were processed using existing Laue approaches, while weaker A2AAR data required an alternative data-processing strategy. This demonstration of the feasibility presents new opportunities for time-resolved experiments with microcrystals to study structural changes in real time at pink-beam synchrotron beamlines worldwide.


X-ray crystallography; injector-based serial crystallography; membrane proteins; pink-beam serial crystallography; protein structures; structural biology; structure determination; third-generation synchrotrons

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