From femtoseconds to minutes: time-resolved macromolecular crystallography at XFELs and synchrotrons

被引:14
作者
Caramello, Nicolas [1 ,2 ]
Royant, Antoine [1 ,3 ]
机构
[1] European Synchrotron Radiat Facil, Struct Biol Grp, 1 Ave Martyrs,CS 40220, F-38043 Grenoble 9, France
[2] Univ Hamburg, Hamburg Ctr Ultrafast Imaging, HARBOR, Luruper Chaussee 149, D-22761 Hamburg, Germany
[3] Univ Grenoble Alpes, CNRS, Inst Biol Struct IBS, CEA, 71 Ave Martyrs,CS 10090, F-38044 Grenoble 9, France
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2024年 / 80卷
关键词
time-resolved serial crystallography; synchrotrons; XFELs; structural photobiology; reaction-intermediate states; bacteriorhodopsin; cryo-trapping; X-RAY-RADIATION; INDUCED STRUCTURAL-CHANGES; BLUE-LIGHT PHOTORECEPTOR; ROOM-TEMPERATURE; SERIAL CRYSTALLOGRAPHY; ABSORPTION-SPECTROSCOPY; ENZYME CATALYSIS; BINDING DOMAIN; PROTEIN; BACTERIORHODOPSIN;
D O I
10.1107/S2059798323011002
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Over the last decade, the development of time-resolved serial crystallography (TR-SX) at X-ray free-electron lasers (XFELs) and synchrotrons has allowed researchers to study phenomena occurring in proteins on the femtosecond-tominute timescale, taking advantage of many technical and methodological breakthroughs. Protein crystals of various sizes are presented to the X-ray beam in either a static or a moving medium. Photoactive proteins were naturally the initial systems to be studied in TR-SX experiments using pump-probe schemes, where the pump is a pulse of visible light. Other reaction initiations through small-molecule diffusion are gaining momentum. Here, selected examples of XFEL and synchrotron time-resolved crystallography studies will be used to highlight the specificities of the various instruments and methods with respect to time resolution, and are compared with cryo-trapping studies.
引用
收藏
页码:60 / 79
页数:20
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