Serial millisecond crystallography for routine room-temperature structure determination at synchrotrons

Tobias Weinert, Natacha Olieric, Robert Cheng, Steffen Brünle, Daniel James, Dmitry Ozerov, Dardan Gashi, Laura Vera, May Marsh, Kathrin Jaeger, Florian Dworkowski, Ezequiel Panepucci, Shibom Basu, Petr Skopintsev, Andrew S. Doré, Tian Geng, Robert M. Cooke, Mengning Liang, Andrea E. Prota, Valerie Panneels, Przemyslaw Nogly, Ulrich Ermler, Gebhard Schertler, Michael Hennig, Michel O. Steinmetz, Meitian Wang and Jörg Standfuss ()
Additional contact information
Tobias Weinert: Paul Scherrer Institut
Natacha Olieric: Paul Scherrer Institut
Robert Cheng: LeadXpro AG
Steffen Brünle: Max-Planck Institute of Biophysics
Daniel James: Paul Scherrer Institut
Dmitry Ozerov: Paul Scherrer Institut
Dardan Gashi: Paul Scherrer Institut
Laura Vera: Swiss Light Source, Paul Scherrer Institut
May Marsh: Swiss Light Source, Paul Scherrer Institut
Kathrin Jaeger: Paul Scherrer Institut
Florian Dworkowski: Swiss Light Source, Paul Scherrer Institut
Ezequiel Panepucci: Swiss Light Source, Paul Scherrer Institut
Shibom Basu: Swiss Light Source, Paul Scherrer Institut
Petr Skopintsev: Paul Scherrer Institut
Andrew S. Doré: Heptares Therapeutics Ltd
Tian Geng: Heptares Therapeutics Ltd
Robert M. Cooke: Heptares Therapeutics Ltd
Mengning Liang: SLAC National Accelerator Laboratory
Andrea E. Prota: Paul Scherrer Institut
Valerie Panneels: Paul Scherrer Institut
Przemyslaw Nogly: Paul Scherrer Institut
Ulrich Ermler: Max-Planck Institute of Biophysics
Gebhard Schertler: Paul Scherrer Institut
Michael Hennig: LeadXpro AG
Michel O. Steinmetz: Paul Scherrer Institut
Meitian Wang: Swiss Light Source, Paul Scherrer Institut
Jörg Standfuss: Paul Scherrer Institut

Nature Communications, 2017, vol. 8, issue 1, 1-11

Abstract: Abstract Historically, room-temperature structure determination was succeeded by cryo-crystallography to mitigate radiation damage. Here, we demonstrate that serial millisecond crystallography at a synchrotron beamline equipped with high-viscosity injector and high frame-rate detector allows typical crystallographic experiments to be performed at room-temperature. Using a crystal scanning approach, we determine the high-resolution structure of the radiation sensitive molybdenum storage protein, demonstrate soaking of the drug colchicine into tubulin and native sulfur phasing of the human G protein-coupled adenosine receptor. Serial crystallographic data for molecular replacement already converges in 1,000–10,000 diffraction patterns, which we collected in 3 to maximally 82 minutes. Compared with serial data we collected at a free-electron laser, the synchrotron data are of slightly lower resolution, however fewer diffraction patterns are needed for de novo phasing. Overall, the data we collected by room-temperature serial crystallography are of comparable quality to cryo-crystallographic data and can be routinely collected at synchrotrons.

Date: 2017
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-00630-4

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DOI: 10.1038/s41467-017-00630-4

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