
Purification, crystallization and preliminary X‐ray analysis of Hsp33 from Saccharomyces cerevisiae
Author(s) -
Liu Wei,
Zhou YeYun,
Teng MaiKun,
Zhou CongZhao
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107000681
Subject(s) - saccharomyces cerevisiae , crystallization , yeast , solvent , crystallography , crystal (programming language) , shock (circulatory) , chemistry , materials science , resolution (logic) , diffusion , biochemistry , thermodynamics , physics , medicine , organic chemistry , artificial intelligence , computer science , programming language
The heat‐shock protein Hsp33 from the yeast Saccharomyces cerevisiae has been overexpressed, purified and crystallized. A crystal was obtained using the hanging‐drop vapour‐diffusion method and a data set was collected to 2.7 Å resolution. The crystal belongs to space group P 4 3 2 1 2, with unit‐cell parameters a = b = 96.43, c = 132.22 Å, α = β = γ = 90°. The asymmetric unit is assumed to contain two subunits of Hsp33, with a V M value of 2.96 Å 3 Da −1 and a solvent content of 58.41%.