{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hull JA"],"funding":["National Research Foundation of Korea"],"pagination":["194-202"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10910541"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["80(Pt 3)"],"pubmed_abstract":["The combination of X-ray free-electron lasers (XFELs) with serial femtosecond crystallography represents cutting-edge technology in structural biology, allowing the study of enzyme reactions and dynamics in real time through the generation of `molecular movies'. This technology combines short and precise high-energy X-ray exposure to a stream of protein microcrystals. Here, the XFEL structure of carbonic anhydrase II, a ubiquitous enzyme responsible for the interconversion of CO<sub>2</sub> and bicarbonate, is reported, and is compared with previously reported NMR and synchrotron X-ray and neutron single-crystal structures."],"journal":["Acta crystallographica. Section D, Structural biology"],"pubmed_title":["XFEL structure of carbonic anhydrase II: a comparative study of XFEL, NMR, X-ray and neutron structures."],"pmcid":["PMC10910541"],"funding_grant_id":["2022R1A2C2091815"],"pubmed_authors":["Hull JA","Park G","Park J","Lee SJ","Kim JK","Lomelino C","Eom I","Park S","Kim M","Hyun H","Andring JT","Lee C","Combs JE","Kim CU","McKenna R","Lim SW"],"additional_accession":[]},"is_claimable":false,"name":"XFEL structure of carbonic anhydrase II: a comparative study of XFEL, NMR, X-ray and neutron structures.","description":"The combination of X-ray free-electron lasers (XFELs) with serial femtosecond crystallography represents cutting-edge technology in structural biology, allowing the study of enzyme reactions and dynamics in real time through the generation of `molecular movies'. This technology combines short and precise high-energy X-ray exposure to a stream of protein microcrystals. Here, the XFEL structure of carbonic anhydrase II, a ubiquitous enzyme responsible for the interconversion of CO<sub>2</sub> and bicarbonate, is reported, and is compared with previously reported NMR and synchrotron X-ray and neutron single-crystal structures.","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Mar","modification":"2026-06-01T08:51:19.786Z","creation":"2025-04-07T11:26:07.606Z"},"accession":"S-EPMC10910541","cross_references":{"pubmed":["38411550"],"doi":["10.1107/s2059798324000482","10.1107/S2059798324000482"]}}