%0 Journal Article
%T XFEL structure of carbonic anhydrase II: a comparative study of XFEL, NMR, X-ray and neutron structures.
%A Hull JA
%A Lee C
%A Kim JK
%A Lim SW
%A Park J
%A Park S
%A Lee SJ
%A Park G
%A Eom I
%A Kim M
%A Hyun H
%A Combs JE
%A Andring JT
%A Lomelino C
%A Kim CU
%A McKenna R
%J Acta Crystallogr D Struct Biol
%V 80
%N 0
%D 2024 Mar 1
%M 38411550
%F 5.699
%R 10.1107/S2059798324000482
%X 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.