ArticleJournal of synchrotron radiation2012
The kinetic dose limit in room-temperature time-resolved macromolecular crystallography.
Article in Journal of synchrotron radiation, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Towards patient-relevant structures: reviewing body-temperature biological macromolecules and their ligands for pharmaceutical applications.Acta crystallographica. Section D, Structural biology · 2026Review
- Data of radiation damage on selenomethionine-substituted single-domain substrate-binding protein.Data in brief · 2024Article
- Biological function investigated by time-resolved structure determination.Structural dynamics (Melville, N.Y.) · 2023Article
- Time-Resolved Macromolecular Crystallography at Pulsed X-ray Sources.International journal of molecular sciences · 2019Review
- A short history of structure based research on the photocycle of photoactive yellow protein.Structural dynamics (Melville, N.Y.) · 2017Review
- Towards time-resolved serial crystallography in a microfluidic device.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Room temperature structures beyond 1.5 Å by serial femtosecond crystallography.Structural dynamics (Melville, N.Y.) · 2015Article
- Time-resolved serial crystallography captures high-resolution intermediates of photoactive yellow protein.Science (New York, N.Y.) · 2014Article
- Microcrystallization techniques for serial femtosecond crystallography using photosystem II from Thermosynechococcus elongatus as a model system.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2014Article
- Protein energy landscapes determined by five-dimensional crystallography.Acta crystallographica. Section D, Biological crystallography · 2013Article
- Kinetic modeling of the X-ray-induced damage to a metalloprotein.The journal of physical chemistry. B · 2013Article
- Laue crystal structure of Shewanella oneidensis cytochrome c nitrite reductase from a high-yield expression system.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2012Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Protein X-ray structures are determined with ionizing radiation that damages the protein at high X-ray doses. As a result, diffraction patterns deteriorate with the increased absorbed dose. Several strategies such as sample freezing or scavenging of X-ray-generated free radicals are currently employed to minimize this damage. However, little is known about how the absorbed X-ray dose affects time-resolved Laue data collected at physiological temperatures where the protein is fully functional in the crystal, and how the kinetic analysis of such data depends on the absorbed dose. Here, direct evidence for the impact of radiation damage on the function of a protein is presented using time-resolved macromolecular crystallography. The effect of radiation damage on the kinetic analysis of time-resolved X-ray data is also explored.
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