Open AccessCrystallization and preliminary X‐ray diffraction studies of the ubiquitin‐like (UbL) domain of the human homologue A of Rad23 (hHR23A) protein
Author(s) -
Chen Yu Wai,
Tajima Toshitaka,
Rees Martin,
GarciaMaya Mitla
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109031376
Subject(s) - crystallography , crystallization , ubiquitin , x ray crystallography , domain (mathematical analysis) , diffraction , materials science , chemistry , physics , biochemistry , optics , organic chemistry , gene , mathematics , mathematical analysis
Human homologue A of Rad23 (hHR23A) plays dual roles in DNA repair as well as serving as a shuttle vehicle targeting polyubiquitinated proteins for degradation. Its N‐terminal ubiquitin‐like (UbL) domain interacts with the 19S proteasomal cap and provides the docking mechanism for protein delivery. Pyramidal crystals of the UbL domain of hHR23A were obtained by the hanging‐drop vapour‐diffusion method with ammonium sulfate as the crystallizing agent. The crystals diffracted to beyond 2 Å resolution and belonged to the hexagonal space group P 6 5 22, with unit‐cell parameters a = b = 78.48, c = 63.57 Å. The structure was solved by molecular replacement using the UbL domain of yeast Dsk2 as the search model.