Ligand Binding: recording events in the active and alternative binding sites using time-resolved crystallography
收藏ESRF Portal2028-01-01 更新2026-04-23 收录
下载链接：
https://doi.esrf.fr/10.15151/ESRF-ES-2008246153
下载链接
链接失效反馈官方服务：
资源简介：
On a molecular level, biological function is closely linked to the dynamic processes of enzymes. However, capturing these conformational changes, especially during catalysis, has proven difficult using conventional experimental methods. Uniquely, time-resolved X-ray crystallography (TRX) can provide insight into these dynamic changes, but is often compounded with substantial experimental challenges. To surmount these challenges and enable TRX on typical beamlines, we have pioneered cryo-trapping TRX. Our SPITROBOT crystal plunger enables to move beyond canonical static imaging of proteins and instead capture short-lived reaction intermediates, that report on dynamic biochemical processes as they unfold. Here we aim to demonstrate that the next generation plunger ‘SPITROBOT-2’ enables reaction quenching within 25 ms and allows following the dynamic events during ligand binding and catalysis for several model systems.
提供机构：
University of Hamburg, Mehrabi Group, Luruper Chaussee 149, Harbor, Geb. 610, 22761 Hamburg, Germany; University Medical Center Hamburg-Eppendorf, Institute of Biochemistry-Signal Transduction, Martinistraße 52, 20246, Hamburg, DE; University Medical Center Hamburg Eppendorf, Institut für Biochemie und Signaltransduktion, Martinistrasse 52, Gebäude N45, Hamburg, 20246 , Hamburg, DE; University of Hamburg, Pearson Group, Luruper Chaussee 149 HARBOR, Building 610, 22761, Hamburg, DE
创建时间：
2028-01-01
