Serial synchrotron and XFEL crystallography for studies of metalloprotein catalysis.

Serial synchrotron and XFEL crystallography for studies of metalloprotein catalysis.
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DOI:
10.1016/j.sbi.2021.07.007
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发表时间:
2021-12
影响因子:
6.8
通讯作者:
Owen RL
Owen RL
中科院分区:
生物学2区
文献类型:
--
作者:
Hough MA;Owen RL

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据估计,所有蛋白质中有一半含有金属,这些金属对各种生物功能都是必不可少的。X射线结晶学是获得这些金属蛋白高分辨率结构的主要方法,但由于辐射损伤的影响,获得完整的结构面临着相当大的挑战。系列结晶学提供了在室温下确定低剂量同步加速器或有效无损伤XFEL结构的前景,并使时间分辨或剂量分辨方法成为可能。互补的光谱数据可以验证金属蛋白晶体中的氧化还原和或配体状态。在这篇文章中,我们讨论了系列结晶学方法在金属蛋白应用方面的发展,并对未来的发展方向进行了评论。
An estimated half of all proteins contain a metal, with these being essential for a tremendous variety of biological functions. X-ray crystallography is the major method for obtaining structures at high resolution of these metalloproteins, but there are considerable challenges to obtain intact structures due to the effects of radiation damage. Serial crystallography offers the prospect of determining low-dose synchrotron or effectively damage free XFEL structures at room temperature and enables time-resolved or dose-resolved approaches. Complementary spectroscopic data can validate redox and or ligand states within metalloprotein crystals. In this opinion, we discuss developments in the application of serial crystallographic approaches to metalloproteins and comment on future directions.
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