ArticleActa crystallographica. Section D, Biological crystallography2011
Can radiation damage to protein crystals be reduced using small-molecule compounds?
Article in Acta crystallographica. Section D, Biological crystallography, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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24 citing papers in PubMed, 45 citations in OpenAlex.
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- B-factor accuracy in protein crystal structures.Acta crystallographica. Section D, Structural biology · 2022Article
- A SAXS-based approach to rationally evaluate radical scavengers - toward eliminating radiation damage in solution and crystallographic studies.Journal of synchrotron radiation · 2021Article
- Radiation damage to biological samples: still a pertinent issue.Journal of synchrotron radiation · 2021Article
- Pulsed 3.5 GHz high power microwaves irradiation on physiological solution and their biological evaluation on human cell lines.Scientific reports · 2021Article
- Pushing the limits of high-resolution polymer microscopy using antioxidants.Nature communications · 2021Article
- Article
- Estimate your dose: RADDOSE-3D.Protein science : a publication of the Protein Society · 2018Article
- Conformational variation of proteins at room temperature is not dominated by radiation damage.Journal of synchrotron radiation · 2017Article
- Quantifying radiation damage in biomolecular small-angle X-ray scattering.Journal of applied crystallography · 2016Article
- In meso in situ serial X-ray crystallography of soluble and membrane proteins at cryogenic temperatures.Acta crystallographica. Section D, Structural biology · 2016Article
- In meso in situ serial X-ray crystallography of soluble and membrane proteins.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Temperature-dependent radiation sensitivity and order of 70S ribosome crystals.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Insights into the mechanism of X-ray-induced disulfide-bond cleavage in lysozyme crystals based on EPR, optical absorption and X-ray diffraction studies.Acta crystallographica. Section D, Biological crystallography · 2013Article
- Effects of cryoprotectants on the structure and thermostability of the human carbonic anhydrase II-acetazolamide complex.Acta crystallographica. Section D, Biological crystallography · 2013Article
- Breaking the radiation damage limit with Cryo-SAXS.Biophysical journal · 2013Article
- To scavenge or not to scavenge, that is STILL the question.Journal of synchrotron radiation · 2013Article
- A survey of global radiation damage to 15 different protein crystal types at room temperature: a new decay model.Journal of synchrotron radiation · 2013Article
- Global radiation damage: temperature dependence, time dependence and how to outrun it.Journal of synchrotron radiation · 2013Article
- Spatial distribution of radiation damage to crystalline proteins at 25-300 K.Acta crystallographica. Section D, Biological crystallography · 2012Article
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4 authors at 2 institutions in 1 country.
Funding
Abstract
Recent studies have defined a data-collection protocol and a metric that provide a robust measure of global radiation damage to protein crystals. Using this protocol and metric, 19 small-molecule compounds (introduced either by cocrystallization or soaking) were evaluated for their ability to protect lysozyme crystals from radiation damage. The compounds were selected based upon their ability to interact with radiolytic products (e.g. hydrated electrons, hydrogen, hydroxyl and perhydroxyl radicals) and/or their efficacy in protecting biological molecules from radiation damage in dilute aqueous solutions. At room temperature, 12 compounds had no effect and six had a sensitizing effect on global damage. Only one compound, sodium nitrate, appeared to extend crystal lifetimes, but not in all proteins and only by a factor of two or less. No compound provided protection at T=100 K. Scavengers are ineffective in protecting protein crystals from global damage because a large fraction of primary X-ray-induced excitations are generated in and/or directly attack the protein and because the ratio of scavenger molecules to protein molecules is too small to provide appreciable competitive protection. The same reactivity that makes some scavengers effective radioprotectors in protein solutions may explain their sensitizing effect in the protein-dense environment of a crystal. A more productive focus for future efforts may be to identify and eliminate sensitizing compounds from crystallization solutions.
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