Journal
NATURE COMMUNICATIONS
Volume 8, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-017-00630-4
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Funding
- SwissFEL
- Swiss National Science Foundation [310030_153145, 31003A_159558]
- European Community's Seventh Framework Program (FP7) [290605]
- ETH Zurich through the NCCR MUST
- ETH FAST programme
- H2020 ITN network X-probe [637295]
- Data Analysis Service project of the Swiss Universities SUC-P2 program [142-004]
- Swiss National Science Foundation (SNF) [310030_153145, 31003A_159558] Funding Source: Swiss National Science Foundation (SNF)
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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.
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