Joshua A Hull, Cheol Lee, Jin Kyun Kim, Seon Woo Lim, Jaehyun Park, Sehan Park, Sang Jae Lee, Gisu Park, Intae Eom, Minseok Kim, HyoJung Hyun, Jacob E Combs, Jacob T Andring, Carrie Lomelino, Chae Un Kim, Robert McKenna
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引用次数: 0
摘要
X 射线自由电子激光器（XFEL）与串行飞秒晶体学的结合代表了结构生物学领域的尖端技术，可通过生成 "分子电影 "实时研究酶的反应和动力学。这项技术结合了对蛋白质微晶体流的短时间和精确的高能 X 射线照射。碳酸酐酶 II 是一种负责二氧化碳和碳酸氢盐相互转化的无处不在的酶，本文报告了碳酸酐酶 II 的 XFEL 结构，并将其与之前报告的核磁共振和同步辐射 X 射线及中子单晶结构进行了比较。
XFEL 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.
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