Data of radiation damage on selenomethionine-substituted single-domain substrate-binding protein

被引:1
|
作者
Nam, Ki Hyun [1 ]
机构
[1] Kookmin Univ, Coll Gen Educ, Seoul 02707, South Korea
来源
DATA IN BRIEF | 2024年 / 53卷
基金
新加坡国家研究基金会;
关键词
Selenomethionine; Radiation damage; Substrate binding protein; Crystal structure; X-ray crystallography; X-RAYS;
D O I
10.1016/j.dib.2024.110114
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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 substratebinding domain from Rhodothermus marinus (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. (c) 2024 The Author(s). Published by Elsevier Inc. This is an open access article under the CC BY license ( http://creativecommons.org/licenses/by/4.0/ )
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页数:9
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