8WXO

Crystal structure of substrate-binding protein from Rhodothermus marinus (Dose III)

Summary for 8WXO

• Entry DOI: 10.2210/pdb8wxo/pdb
• Descriptor: ABC-type uncharacterized transport system periplasmic component-like protein (2 entities in total)
• Functional Keywords: substrate binding protein, protein transport
• Biological source: Rhodothermus marinus DSM 4252
• Total number of polymer chains: 2
• Total formula weight: 36242.81

Authors

Nam, K.H. (deposition date: 2023-10-30, release date: 2023-11-22, Last modification date: 2024-10-16)

Primary citation

Nam, K.H.
Data of radiation damage on selenomethionine-substituted single-domain substrate-binding protein.
Data Brief, 53:110114-110114, 2024

PubMed Abstract: 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.

PubMed: 38348329
DOI: 10.1016/j.dib.2024.110114

Experimental method

X-RAY DIFFRACTION (1.68 Å)