XFEL structure of carbonic anhydrase II: a comparative study of XFEL, NMR, X-ray and neutron structures,Acta Crystallographica Section D

当前位置： X-MOL 学术 › Acta Cryst. D › 论文详情

Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)

XFEL structure of carbonic anhydrase II: a comparative study of XFEL, NMR, X-ray and neutron structures
Acta Crystallographica Section D ( IF 2.6 ) Pub Date : 2024-02-27 , DOI: 10.1107/s2059798324000482
Joshua A Hull ₁ , Cheol Lee ₂ , Jin Kyun Kim ₂ , Seon Woo Lim ₂ , Jaehyun Park ₃ , Sehan Park ₃ , Sang Jae Lee ₃ , Gisu Park ₃ , Intae Eom ₃ , Minseok Kim ₃ , HyoJung Hyun ₃ , Jacob E Combs ₁ , Jacob T Andring ₁ , Carrie Lomelino ₁ , Chae Un Kim ₂ , Robert McKenna ₁

Affiliation

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.

中文翻译：

碳酸酐酶 II 的 XFEL 结构：XFEL、NMR、X 射线和中子结构的比较研究

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的尖端技术，可以通过生成“分子电影”来实时研究酶反应和动力学。该技术将短而精确的高能 X 射线照射到蛋白质微晶流上。本文报道了碳酸酐酶 II（一种负责 CO ₂和碳酸氢盐相互转化的普遍酶）的 XFEL 结构，并与之前报道的 NMR 和同步加速器 X 射线和中子单晶结构进行了比较。

更新日期：2024-02-27

点击分享查看原文

点击收藏

阅读更多本刊新发论文