ArticleIUCrJ2020
Millisecond time-resolved serial oscillation crystallography of a blue-light photoreceptor at a synchrotron.
Article in IUCrJ, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- A simple and practical approach for protein serial crystallography using grease matrix and large-area support film.Journal of synchrotron radiation · 2026Article
- Conserved structural motifs in PAS, LOV, and CRY proteins regulate circadian rhythms and are therapeutic targets.FEBS letters · 2026Review
- Current and future perspectives for structural biology at the Grenoble EPN campus: a comprehensive overview.Journal of synchrotron radiation · 2025Review
- Article
- The time revolution in macromolecular crystallography.Structural dynamics (Melville, N.Y.) · 2024Article
- From femtoseconds to minutes: time-resolved macromolecular crystallography at XFELs and synchrotrons.Acta crystallographica. Section D, Structural biology · 2024Article
- Guide to serial synchrotron crystallography.Current research in structural biology · 2024Review
- Combining on-line spectroscopy with synchrotron and X-ray free electron laser crystallography.Current opinion in structural biology · 2023Review
- Slow protein dynamics probed by time-resolved oscillation crystallography at room temperature.IUCrJ · 2022Article
- Probing ligand binding of endothiapepsin by `temperature-resolved' macromolecular crystallography.Acta crystallographica. Section D, Structural biology · 2022Article
- Evaluation of the data-collection strategy for room-temperature micro-crystallography studied by serial synchrotron rotation crystallography combined with the humid air and glue-coating method.Acta crystallographica. Section D, Structural biology · 2021Article
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Authors and funding
6 authors.
Funding
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Abstract
The recent development of serial crystallography has popularized time-resolved crystallography as a technique to determine the structure of protein-reaction intermediate states. However, most approaches rely on the availability of thousands to millions of microcrystals. A method is reported here, using monochromatic synchrotron radiation, for the room-temperature collection, processing and merging of X-ray oscillation diffraction data from <100 samples in order to observe the build up of a photoreaction intermediate species. Using this method, we monitored with a time resolution of 63 ms how the population of a blue-light photoreceptor domain in a crystal progressively photoconverts from the dark to the light state. The series of resulting snapshots allows us to visualize in detail the gradual rearrangement of both the protein and chromophore during this process.
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Registered trials
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