ArticleActa crystallographica. Section D, Biological crystallography2014
Temperature-dependent radiation sensitivity and order of 70S ribosome crystals.
Article in Acta crystallographica. Section D, Biological crystallography, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Extending the reach of single-particle cryoEM.Current opinion in structural biology · 2025Review
- Reducing the effects of radiation damage in cryo-EM using liquid helium temperatures.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Specific radiation damage to halogenated inhibitors and ligands in protein-ligand crystal structures.Journal of applied crystallography · 2024Article
- Determining biomolecular structures near room temperature using X-ray crystallography: concepts, methods and future optimization.Acta crystallographica. Section D, Structural biology · 2023Article
- On the reduction in the effects of radiation damage to two-dimensional crystals of organic and biological molecules at liquid-helium temperature.Ultramicroscopy · 2022Article
- Integrated sample-handling and mounting system for fixed-target serial synchrotron crystallography.Acta crystallographica. Section D, Structural biology · 2021Article
- Doses for experiments with microbeams and microcrystals: Monte Carlo simulations in RADDOSE-3D.Protein science : a publication of the Protein Society · 2021Article
- Cryo-EM with sub-1 Å specimen movement.Science (New York, N.Y.) · 2020Article
- Radiation damage and dose limits in serial synchrotron crystallography at cryo- and room temperatures.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
- Structure of the 30S ribosomal decoding complex at ambient temperature.RNA (New York, N.Y.) · 2018Article
- Comparison of Flattening Filter and Flattening Filter-Free Volumetric Modulated Arc Radiotherapy in Patients with Locally Advanced Nasopharyngeal Carcinoma.Medical science monitor : international medical journal of experimental and clinical research · 2018Article
- Enzyme catalysis captured using multiple structures from one crystal at varying temperatures.IUCrJ · 2018Article
- Article
- Atomic structure of granulin determined from native nanocrystalline granulovirus using an X-ray free-electron laser.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Concentric-flow electrokinetic injector enables serial crystallography of ribosome and photosystem II.Nature methods · 2016Article
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5 authors.
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Abstract
All evidence to date indicates that at T = 100 K all protein crystals exhibit comparable sensitivity to X-ray damage when quantified using global metrics such as change in scaling B factor or integrated intensity versus dose. This is consistent with observations in cryo-electron microscopy, and results because nearly all diffusive motions of protein and solvent, including motions induced by radiation damage, are frozen out. But how do the sensitivities of different proteins compare at room temperature, where radiation-induced radicals are free to diffuse and protein and lattice structures are free to relax in response to local damage? It might be expected that a large complex with extensive conformational degrees of freedom would be more radiation sensitive than a small, compact globular protein. As a test case, the radiation sensitivity of 70S ribosome crystals has been examined. At T = 100 and 300 K, the half doses are 64 MGy (at 3 Å resolution) and 150 kGy (at 5 Å resolution), respectively. The maximum tolerable dose in a crystallography experiment depends upon the initial or desired resolution. When differences in initial data-set resolution are accounted for, the former half dose is roughly consistent with that for model proteins, and the 100/300 K half-dose ratio is roughly a factor of ten larger. 70S ribosome crystals exhibit substantially increased resolution at 100 K relative to 300 K owing to cooling-induced ordering and not to reduced radiation sensitivity and slower radiation damage.
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