Department of Biochemistry and Molecular Biology, College of Medicine, University of Florida, Gainesville, FL 32610, USA.
Department of Physics, Ulsan National Institute of Science and Technology (UNIST), Ulsan 44919, Republic of Korea.
Acta Crystallogr D Struct Biol. 2024 Mar 1;80(Pt 3):194-202. doi: 10.1107/S2059798324000482. Epub 2024 Feb 27.
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 and bicarbonate, is reported, and is compared with previously reported NMR and synchrotron X-ray and neutron single-crystal structures.
X 射线自由电子激光（XFEL）与连续飞秒晶体学的结合代表了结构生物学的前沿技术，通过生成“分子电影”，可以实时研究酶反应和动力学。该技术将短而精确的高能 X 射线照射与蛋白质微晶体流相结合。本文报道了碳酸酐酶 II 的 XFEL 结构，碳酸酐酶 II 是一种普遍存在的酶，负责 CO 和碳酸氢盐的相互转化，并与之前报道的 NMR 和同步辐射 X 射线和中子单晶结构进行了比较。
