Nam Ki Hyun
College of General Education, Kookmin University, Seoul 02707, South Korea.
Data Brief. 2024 Jan 30;53:110114. doi: 10.1016/j.dib.2024.110114. eCollection 2024 Apr.
Radiation damage is an inherent issue in X-ray crystallography. It not only damages macromolecular crystals, which lowers the quality of the diffraction intensity, but results in inaccurate structural information. Among the various types of radiation damage, little is known regarding the damage to selenomethionine, an amino acid contained in some proteins. Recently, radiation damage to the selenomethionine-substituted single-domain substrate-binding domain from (SeMet-RmSBP) was investigated. Global and specific radiation damage from four datasets collected by repeatedly exposing a single RmSBP-SeMet crystal to X-rays were analyzed. The results indicated that the B-factor value of the selenium atom in selenomethionine was significantly increased compared with other atoms. To date, no images of radiation damage have been reported for selenomethionine-substituted proteins. Therefore, these data may be used to study radiation damage in macromolecular crystallography. This study provides insight into radiation damage associated with selenomethionine.
辐射损伤是X射线晶体学中一个固有的问题。它不仅会破坏大分子晶体，降低衍射强度的质量，还会导致结构信息不准确。在各种类型的辐射损伤中，对于某些蛋白质中所含的氨基酸硒代蛋氨酸的损伤了解甚少。最近，对来自[具体来源未提及]的硒代蛋氨酸取代的单结构域底物结合结构域（SeMet-RmSBP）的辐射损伤进行了研究。分析了通过反复将单个RmSBP-SeMet晶体暴露于X射线而收集的四个数据集的整体和特定辐射损伤。结果表明，与其他原子相比，硒代蛋氨酸中硒原子的B因子值显著增加。迄今为止，尚未报道过硒代蛋氨酸取代蛋白质的辐射损伤图像。因此，这些数据可用于研究大分子晶体学中的辐射损伤。这项研究为与硒代蛋氨酸相关的辐射损伤提供了见解。
