Body temperature protein X-ray crystallography at 37°C: A rhenium protein complex seeking a physiological condition structure: Raw Diffraction Images (112 week soak) Zenodo

The labratory dataset of the raw diffraction images obtained after 112 weeks of soaking in the mother liquor and collected at a wavelength of 1.54 Å, illustrating the covalent coordination of the rhenium(I) tricarbonyl fragment to the His and Asp amino acid residues as well as other similarities when comparing the 37°C data set to 100K data set as described in the publication titled "Body temperature protein X-ray crystallography at 37°C: A rhenium protein complex seeking a physiological condition structure", written by Jacobs, Helliwell & Brink, ChemComm, 2024. The raw diffraction images for the labratory data sets are made available at the Zenodo research data archive, as specified in the publication.本实验室数据集包含在母液（mother liquor）中浸泡112周后采集的原始衍射图像（raw diffraction images），采集波长为1.54埃（Å）。该数据集阐释了三羰基合铼(I)（rhenium(I) tricarbonyl）片段与组氨酸（His）、天冬氨酸（Asp）氨基酸残基（amino acid residues）的共价配位（covalent coordination）作用，并对比了37℃数据集（37°C data set）与100K数据集（100K data set）之间的其他相似性。相关研究内容见于Jacobs、Helliwell与Brink于2024年发表在《化学通讯（ChemComm）》上的学术论文《37℃体温下的蛋白质X射线晶体学：寻求生理条件结构的铼蛋白复合物》。如该论文所述，本实验室数据集对应的原始衍射图像已上传至Zenodo科研数据存档平台供公开获取。