{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Greisman JB"],"funding":["Searle Scholars Program","Burroughs Wellcome Fund","New York Community Trust","NIGMS NIH HHS","National Science Foundation"],"pagination":["986-996"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9344477"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["78(Pt 8)"],"pubmed_abstract":["Single-wavelength anomalous diffraction (SAD) is a routine method for overcoming the phase problem when solving macromolecular structures. This technique requires the accurate measurement of intensities to determine differences between Bijvoet pairs. Although SAD experiments are commonly conducted at cryogenic temperatures to mitigate the effects of radiation damage, such temperatures can alter the conformational ensemble of the protein and may impede the merging of data from multiple crystals due to non-uniform freezing. Here, a strategy is presented to obtain high-quality data from room-temperature, single-crystal experiments. To illustrate the strengths of this approach, native SAD phasing at 6.55 keV was used to solve four structures of three model systems at 295 K. The resulting data sets allow automatic phasing and model building, and reveal alternate conformations that reflect the structure of proteins at room temperature."],"journal":["Acta crystallographica. Section D, Structural biology"],"pubmed_title":["Native SAD phasing at room temperature."],"pmcid":["PMC9344477"],"funding_grant_id":["DP2 GM141000","DGE1745303","P30 GM124165","338034","SSP-2018-3240"],"pubmed_authors":["Greisman JB","Klureza MA","Kurinov I","Hekstra DR","Sheehan CJ","Dalton KM"],"additional_accession":[]},"is_claimable":false,"name":"Native SAD phasing at room temperature.","description":"Single-wavelength anomalous diffraction (SAD) is a routine method for overcoming the phase problem when solving macromolecular structures. This technique requires the accurate measurement of intensities to determine differences between Bijvoet pairs. Although SAD experiments are commonly conducted at cryogenic temperatures to mitigate the effects of radiation damage, such temperatures can alter the conformational ensemble of the protein and may impede the merging of data from multiple crystals due to non-uniform freezing. Here, a strategy is presented to obtain high-quality data from room-temperature, single-crystal experiments. To illustrate the strengths of this approach, native SAD phasing at 6.55 keV was used to solve four structures of three model systems at 295 K. The resulting data sets allow automatic phasing and model building, and reveal alternate conformations that reflect the structure of proteins at room temperature.","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Aug","modification":"2026-05-09T13:57:52.256Z","creation":"2026-05-05T03:06:25.102Z"},"accession":"S-EPMC9344477","cross_references":{"pubmed":["35916223"],"doi":["10.1107/S2059798322006799","10.1107/s2059798322006799"]}}