Open AccessPurification, crystallization and preliminary X‐ray crystallographic analysis of the human heat‐shock protein 40 Hdj1 and its C‐terminal peptide‐binding domain
Author(s) -
Suzuki Hironori,
Noguchi Shuji,
Arakawa Hiroshi,
Tokida Tadaaki,
Hashimoto Mariko,
Satow Yoshinori
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110034081
Subject(s) - crystallization , peptide , crystallography , resolution (logic) , ctd , hsp70 , diffraction , c terminus , x ray crystallography , heat shock protein , chemistry , biochemistry , amino acid , physics , optics , geology , oceanography , organic chemistry , artificial intelligence , computer science , gene
Hsp40 is a co‐chaperone of Hsp70 that correctly folds polypeptides that exist in non‐native forms. The C‐terminal peptide‐binding domain (CTD) of the human Hsp40 Hdj1 has been purified and crystallized. In the presence of the C‐terminal octapeptide of human Hsp70, four types of crystals, types I‐B, II, III and IV, were grown and diffracted to 1.85, 2.51, 2.10 and 2.80 Å resolution, respectively. In the absence of the octapeptide, type I‐A crystals of the CTD were grown that diffracted to 2.05 Å resolution. The full‐length Hdj1 was also purified and crystallized (type V crystals); the crystal diffracted to 3.90 Å resolution.