Exploring the differences in the structural characterisation of inhibitor binding between cryo- and room-temperature using multicrystal X-ray crystall

在基于结构的药物设计中使用的大多数结合蛋白质结构是使用在低温下收集的单晶的晶体学数据来确定的。然而，它仍然难以常规获得足够大的高分辨率数据收集的单个蛋白质晶体。该项目旨在研究多晶体，室温X射线晶体学，其中来自许多小晶体的X射线数据在室温下收集并合并为一个完整的数据集，是否适合应用于基于结构的药物设计。将研究在低温和室温下收集的数据之间的化合物结合和X射线诱导的辐射损伤结合配体的差异。

Most inhibitor-bound protein structures used in structure-based drug design are determined using crystallographic data from single crystals collected at cryogenic temperatures. However, it remains difficult to routinely obtain single protein crystals large enough for high resolution data collection. This project aims to investigate if multicrystal, room temperature X-ray crystallography, in which X-ray data from many small crystals is collected at room temperature and merged to a complete dataset, is suitable for application in structure-based drug design. Differences in compound binding and differences in X-ray induced radiation damage to bound ligands between data collected at cryogenic- and room-temperature will be investigated.