ArticleNature communications2017
Serial millisecond crystallography for routine room-temperature structure determination at synchrotrons.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 132 papers.
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Who cites it
132 citing papers in PubMed, 264 citations in OpenAlex.
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- Evolution of macromolecular crystallography beamlines at the Swiss Light Source and SwissFEL.Journal of synchrotron radiation · 2025Article
- Macromolecular crystallography and biology at the Linac Coherent Light Source.Journal of synchrotron radiation · 2025Article
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- Novel fixed-target serial crystallography flip-holder for macromolecular crystallography beamlines at synchrotron radiation sources.Journal of synchrotron radiation · 2025Article
- Structural Insights Into the Opening Mechanism of C1C2 Channelrhodopsin.Journal of the American Chemical Society · 2025Article
- Advancing macromolecular structure determination with microsecond X-ray pulses at a 4th generation synchrotron.Communications chemistry · 2025Article
- Effect of crystal-to-detector distance shift on data processing in serial crystallography.PloS one · 2025Article
- Photoswitch dissociation from a G protein-coupled receptor resolved by time-resolved serial crystallography.Nature communications · 2024Article
- Scaling and merging time-resolved pink-beam diffraction with variational inference.Structural dynamics (Melville, N.Y.) · 2024Article
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- In situ serial crystallography facilitates 96-well plate structural analysis at low symmetry.IUCrJ · 2024Article
- Monitoring GPCR conformation with GFP-inspired dyes.iScience · 2024Article
72 more citing papers are in PubMed but not listed here.
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Authors and funding
27 authors at 6 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
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.Serial crystallography was developed for protein crystal data collection with X-ray free-electron lasers. Here the authors present several examples which show that serial crystallography using high-viscosity injectors can also be routinely employed for room-temperature data collection at synchrotrons.
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Registered trials
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