XFEL structure of carbonic anhydrase II: a comparative study of XFEL, NMR, X-ray and neutron structures
Acta Crystallographica Section D: Structural Biology, 2024•journals.iucr.org
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 ofmolecular 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 …
crystallography represents cutting-edge technology in structural biology, allowing the study
of enzyme reactions and dynamics in real time through the generation ofmolecular 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 …
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.
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