ReviewJournal of synchrotron radiation2015
Identifying and quantifying radiation damage at the atomic level.
Review in Journal of synchrotron radiation, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
28 citing papers in PubMed.
- Separating the effects of temperature and absorbed X-ray dose on unit-cell volume.Acta crystallographica. Section D, Structural biology · 2026Article
- It started off as a Cys, how did it end up like this? Identifying the extent of unmodelled oxidatively modified cysteines within the Protein Data Bank.Acta crystallographica. Section D, Structural biology · 2026Article
- Radiation damage in sub-Ångström resolution macromolecular crystallography: a low-dose study.Acta crystallographica. Section D, Structural biology · 2026Article
- Limiting the effects of radiation damage in MicroED through dose selection during data processing.Acta crystallographica. Section D, Structural biology · 2025Article
- Doses for X-ray and electron diffraction: New features in RADDOSE-3D including intensity decay models.Protein science : a publication of the Protein Society · 2024Article
- Identifying and avoiding radiation damage in macromolecular crystallography.Acta crystallographica. Section D, Structural biology · 2024Article
- Using graphlet degree vectors to predict atomic displacement parameters in protein structures.Acta crystallographica. Section D, Structural biology · 2023Article
- Rapid and efficient ambient temperature X-ray crystal structure determination at Turkish Light Source.Scientific reports · 2023Article
- Serial macromolecular crystallography at ALBA Synchrotron Light Source.Journal of synchrotron radiation · 2022Article
- Quantifying and comparing radiation damage in the Protein Data Bank.Nature communications · 2022Article
- Uses and Abuses of the Atomic Displacement Parameters in Structural Biology.Methods in molecular biology (Clifton, N.J.) · 2022Article
- B-factor accuracy in protein crystal structures.Acta crystallographica. Section D, Structural biology · 2022Article
- Structure of Usutu virus SAAR-1776 displays fusion loop asymmetry.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- The copper(II)-binding tripeptide GHK, a valuable crystallization and phasing tag for macromolecular crystallography.Acta crystallographica. Section D, Structural biology · 2020Article
- Crystallization and structure of ebselen bound to Cys141 of human inositol monophosphatase.Acta crystallographica. Section F, Structural biology communications · 2020Article
- The susceptibility of disulfide bonds towards radiation damage may be explained by S⋯O interactions.IUCrJ · 2020Article
- Review
- SAXS studies of X-ray induced disulfide bond damage: Engineering high-resolution insight from a low-resolution technique.PloS one · 2020Article
- Unravelling the covalent binding of zampanolide and taccalonolide AJ to a minimalist representation of a human microtubule.Journal of computer-aided molecular design · 2019Article
- Structural knowledge or X-ray damage? A case study on xylose isomerase illustrating both.Journal of synchrotron radiation · 2019Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Radiation damage impedes macromolecular diffraction experiments. Alongside the well known effects of global radiation damage, site-specific radiation damage affects data quality and the veracity of biological conclusions on protein mechanism and function. Site-specific radiation damage follows a relatively predetermined pattern, in that different structural motifs are affected at different dose regimes: in metal-free proteins, disulfide bonds tend to break first followed by the decarboxylation of aspartic and glutamic acids. Even within these damage motifs the decay does not progress uniformly at equal rates. Within the same protein, radiation-induced electron density decay of a particular chemical group is faster than for the same group elsewhere in the protein: an effect known as preferential specific damage. Here, BDamage, a new atomic metric, is defined and validated to recognize protein regions susceptible to specific damage and to quantify the damage at these sites. By applying BDamage to a large set of known protein structures in a statistical survey, correlations between the rates of damage and various physicochemical parameters were identified. Results indicate that specific radiation damage is independent of secondary protein structure. Different disulfide bond groups (spiral, hook, and staple) show dissimilar radiation damage susceptibility. There is a consistent positive correlation between specific damage and solvent accessibility.
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