X射线
碳酸酐酶
中子
结晶学
化学
物理
核磁共振
核物理学
酶
作者
Joshua A. Hull,Cheol Lee,Jin Kyun Kim,Sujeong Lim,Jaehyun Park,Sehan Park,Sang Jae Lee,Gisu Park,Intae Eom,Minseok Kim,H.J. Hyun,Jacob Combs,Jacob T. Andring,Carrie L. Lomelino,Chae Un Kim,Robert McKenna
标识
DOI:10.1107/s2059798324000482
摘要
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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