biostudies-literatureHull JANational Research Foundation of Korea194-202https://www.ebi.ac.uk/biostudies/studies/S-EPMC10910541biostudies-literatureUnknown80(Pt 3)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.Acta crystallographica. Section D, Structural biologyXFEL structure of carbonic anhydrase II: a comparative study of XFEL, NMR, X-ray and neutron structures.PMC109105412022R1A2C2091815Hull JAPark GPark JLee SJKim JKLomelino CEom IPark SKim MHyun HAndring JTLee CCombs JEKim CUMcKenna RLim SWfalseXFEL structure of carbonic anhydrase II: a comparative study of XFEL, NMR, X-ray and neutron structures.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 CO₂ and bicarbonate, is reported, and is compared with previously reported NMR and synchrotron X-ray and neutron single-crystal structures.2024-01-01T00:00:00Z2024 Mar2026-06-01T08:51:19.786Z2025-04-07T11:26:07.606ZS-EPMC109105413841155010.1107/s205979832400048210.1107/S2059798324000482