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

Weinert, T., Olieric, N., Cheng, R., Brünle, S., James, D., Ozerov, D., et al. (2017). Serial millisecond crystallography for routine room-temperature structure determination at synchrotrons. Nature Communications, 8: 542. doi:10.1038/s41467-017-00630-4.

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 Creators:
Weinert, Tobias1, Author
Olieric, Natacha1, Author
Cheng, Robert2, Author
Brünle, Steffen3, Author           
James, Daniel1, Author
Ozerov, Dmitry4, Author
Gashi, Dardan1, 5, Author
Vera, Laura6, Author
Marsh, May6, Author
Jaeger, Kathrin1, Author
Dworkowski, Florian6, Author
Panepucci, Ezequiel6, Author
Basu, Shibom6, Author
Skopintsev, Petr1, Author
Dorè, Andrew S.7, Author
Geng, Tian7, Author
Cooke, Robert M.7, Author
Liang, Mengning8, Author
Prota, Andrea E.1, Author
Paneels, Valerie1, Author
Nogly, Przemyslaw1, AuthorErmler, Ulrich3, Author           Schertler, Gebhard1, 9, AuthorHennig, Michael2, AuthorSteinmetz, Michel O.1, 10, AuthorWang, Meitian6, AuthorStandfuss, Jörg1, Author more..
Affiliations:
1Laboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institut, 5232 Villigen PSI, Switzerland, ou_persistent22              
2LeadXpro AG, Park InnovAARE, 5234 Villigen PSI, Switzerland, ou_persistent22              
3Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
4Science IT, Paul Scherrer Institut, 5232 Villigen PSI, Switzerland, ou_persistent22              
5SwissFEL, Paul Scherrer Institut, 5232 Villigen PSI, Switzerland, ou_persistent22              
6Macromolecular Crystallography, Swiss Light Source, Paul Scherrer Institut, 5232 Villigen PSI, Switzerland, ou_persistent22              
7Heptares Therapeutics Ltd, Biopark Broadwater Road, Welwyn Garden City AL7 3AX, UK, ou_persistent22              
8Linac Coherent Light Source, SLAC National Accelerator Laboratory, 2575 Sand Hill Road, Menlo Park, CA 94025, USA, ou_persistent22              
9Department of Biology, ETH Zurich, 8093 Zürich, Switzerland, ou_persistent22              
10University of Basel, Biozentrum, Basel 4056, Switzerland, ou_persistent22              

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 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.

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Language(s): eng - English
 Dates: 2017-03-302017-07-142017-09-14
 Publication Status: Published online
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/s41467-017-00630-4
 Degree: -

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Title: Nature Communications
  Abbreviation : Nat. Commun.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 8 Sequence Number: 542 Start / End Page: - Identifier: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723