The time revolution in macromolecular crystallography

被引:1
|
作者
Khusainov, Georgii [1 ]
Standfuss, Joerg [1 ]
Weinert, Tobias [1 ]
机构
[1] Paul Scherrer Inst, Div Biol & Chem, Lab Biomol Res, Villigen, Switzerland
来源
STRUCTURAL DYNAMICS-US | 2024年 / 11卷 / 02期
基金
瑞士国家科学基金会;
关键词
SERIAL FEMTOSECOND CRYSTALLOGRAPHY; PHOTOACTIVE YELLOW PROTEIN; INDUCED STRUCTURAL-CHANGES; RAY LAUE DIFFRACTION; RESOLVED CRYSTALLOGRAPHY; SYNCHROTRON-RADIATION; MILLISECOND CRYSTALLOGRAPHY; LIGAND MIGRATION; SAMPLE DELIVERY; CARBON-MONOXIDE;
D O I
10.1063/4.0000247
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
Macromolecular crystallography has historically provided the atomic structures of proteins fundamental to cellular functions. However, the advent of cryo-electron microscopy for structure determination of large and increasingly smaller and flexible proteins signaled a paradigm shift in structural biology. The extensive structural and sequence data from crystallography and advanced sequencing techniques have been pivotal for training computational models for accurate structure prediction, unveiling the general fold of most proteins. Here, we present a perspective on the rise of time-resolved crystallography as the new frontier of macromolecular structure determination. We trace the evolution from the pioneering time-resolved crystallography methods to modern serial crystallography, highlighting the synergy between rapid detection technologies and state-of-the-art x-ray sources. These innovations are redefining our exploration of protein dynamics, with high-resolution crystallography uniquely positioned to elucidate rapid dynamic processes at ambient temperatures, thus deepening our understanding of protein functionality. We propose that the integration of dynamic structural data with machine learning advancements will unlock predictive capabilities for protein kinetics, revolutionizing dynamics like macromolecular crystallography revolutionized structural biology.
引用
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页数:17
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