Serial millisecond crystallography for routine room-temperature structure determination at synchrotrons.
Saved in:
| Online Access: |
Full Text (via OSTI) |
|---|---|
| Format: | eBook |
| Language: | English |
| Published: |
Washington, D.C. : Oak Ridge, Tenn. :
United States. Department of Energy. Office of Science ; Distributed by the Office of Scientific and Technical Information, U.S. Department of Energy,
2017.
|
| Subjects: |
| 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. |
|---|---|
| Item Description: | Published through Scitech Connect. 09/14/2017. "Journal ID: ISSN 2041-1723." "Other: PII: 630." Weinert, Tobias ; Olieric, Natacha ; Cheng, Robert ; Brünle, Steffen ; James, Daniel ; Ozerov, Dmitry ; Gashi, Dardan ; Vera, Laura ; Marsh, May ; Jaeger, Kathrin ; et al; SLAC National Accelerator Lab., Menlo Park, CA (United States) |
| Physical Description: | Size: Article number: 542 : digital, PDF file. |