ArticleIUCrJ2019
Specific radiation damage is a lesser concern at room temperature.
Article in IUCrJ, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
- Serendipitous crystal structure of mJuniper, a rationally designed cyan fluorescent protein.Acta crystallographica. Section F, Structural biology communications · 2026Article
- Structural evidence of thioacetate reduction by fluorescent protein mRuby.European biophysics journal : EBJ · 2026Article
- Radiation-induced peroxide rupture and its temperature-dependent repair probed by homogeneous X-ray irradiation.Acta crystallographica. Section D, Structural biology · 2026Article
- Mapping the effects of specific radiation damage and solvent radiolysis in buffers and crystals with online UV-Vis absorption spectroscopy.Acta crystallographica. Section D, Structural biology · 2026Article
- Article
- Coupled on-line in crystallo UV-Vis absorption spectroscopy and X-ray crystallography to compare specific radiation damage in metal-containing proteins at room versus cryogenic temperature.Acta crystallographica. Section D, Structural biology · 2026Article
- TheJournal of applied crystallography · 2025Article
- Revealing Functional Hotspots: Temperature-Dependent Crystallography of K-RAS Highlights Allosteric and Druggable Sites.bioRxiv : the preprint server for biology · 2025Article
- Article
- Identifying and avoiding radiation damage in macromolecular crystallography.Acta crystallographica. Section D, Structural biology · 2024Article
- From femtoseconds to minutes: time-resolved macromolecular crystallography at XFELs and synchrotrons.Acta crystallographica. Section D, Structural biology · 2024Article
- Article
- A simple goniometer-compatible flow cell for serial synchrotron X-ray crystallography.Journal of applied crystallography · 2023Article
- Microfluidic rotating-target device capable of three-degrees-of-freedom motion for efficient in situ serial synchrotron crystallography.Journal of synchrotron radiation · 2023Article
- Determining biomolecular structures near room temperature using X-ray crystallography: concepts, methods and future optimization.Acta crystallographica. Section D, Structural biology · 2023Article
- Slow protein dynamics probed by time-resolved oscillation crystallography at room temperature.IUCrJ · 2022Article
- Rapid and efficient room-temperature serial synchrotron crystallography using the CFEL TapeDrive.IUCrJ · 2022Article
- Article
- Megahertz pulse trains enable multi-hit serial femtosecond crystallography experiments at X-ray free electron lasers.Nature communications · 2022Article
- Probing ligand binding of endothiapepsin by `temperature-resolved' macromolecular crystallography.Acta crystallographica. Section D, Structural biology · 2022Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Carrying out macromolecular crystallography (MX) experiments at cryogenic temperatures significantly slows the rate of global radiation damage, thus facilitating the solution of high-resolution crystal structures of macromolecules. However, cryo-MX experiments suffer from the early onset of so-called specific radiation damage that affects certain amino-acid residues and, in particular, the active sites of many proteins. Here, a series of MX experiments are described which suggest that specific and global radiation damage are much less decoupled at room temperature than they are at cryogenic temperatures. The results reported here demonstrate the interest in reviving the practice of collecting MX diffraction data at room temperature and allow structural biologists to favourably envisage the development of time-resolved MX experiments at synchrotron sources.
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