{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Yabukarski F"],"funding":["Stanford University","Human Frontier Science Program","NIGMS NIH HHS","National Science Foundation"],"pagination":["945-963"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9344472"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["78(Pt 8)"],"pubmed_abstract":["Cryo-cooling has been nearly universally adopted to mitigate X-ray damage and facilitate crystal handling in protein X-ray crystallography. However, cryo X-ray crystallographic data provide an incomplete window into the ensemble of conformations that is at the heart of protein function and energetics. Room-temperature (RT) X-ray crystallography provides accurate ensemble information, and recent developments allow conformational heterogeneity (the experimental manifestation of ensembles) to be extracted from single-crystal data. Nevertheless, high sensitivity to X-ray damage at RT raises concerns about data reliability. To systematically address this critical issue, increasingly X-ray-damaged high-resolution data sets (1.02-1.52 Å resolution) were obtained from single proteinase K, thaumati"],"journal":["Acta crystallographica. Section D, Structural biology"],"pubmed_title":["Evaluating the impact of X-ray damage on conformational heterogeneity in room-temperature (277 K) and cryo-cooled protein crystals."],"pmcid":["PMC9344472"],"funding_grant_id":["P41 GM103393","MCB-1714723"],"pubmed_authors":["Yabukarski F","Du S","Mokhtari DA","Doukov T","Herschlag D"],"additional_accession":[]},"is_claimable":false,"name":"Evaluating the impact of X-ray damage on conformational heterogeneity in room-temperature (277 K) and cryo-cooled protein crystals.","description":"Cryo-cooling has been nearly universally adopted to mitigate X-ray damage and facilitate crystal handling in protein X-ray crystallography. However, cryo X-ray crystallographic data provide an incomplete window into the ensemble of conformations that is at the heart of protein function and energetics. Room-temperature (RT) X-ray crystallography provides accurate ensemble information, and recent developments allow conformational heterogeneity (the experimental manifestation of ensembles) to be extracted from single-crystal data. Nevertheless, high sensitivity to X-ray damage at RT raises concerns about data reliability. To systematically address this critical issue, increasingly X-ray-damaged high-resolution data sets (1.02-1.52 Å resolution) were obtained from single proteinase K, thaumati","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Aug","modification":"2026-05-09T14:02:33.402Z","creation":"2024-11-13T21:35:22.431Z"},"accession":"S-EPMC9344472","cross_references":{"pubmed":["35916220"],"doi":["10.1107/s2059798322005939","10.1107/S2059798322005939"]}}