Cloning, purification, crystallization and preliminary X-ray studies of HMO2 from Saccharomyces cerevisiae.

ABSTRACT: The high-mobility group protein (HMO2) of Saccharomyces cerevisiae is a component of the chromatin-remodelling complex INO80, which is involved in double-strand break (DSB) repair. HMO2 can also bind DNA to protect it from exonucleolytic cleavage. Nevertheless, little structural information is available regarding these functions of HMO2. Since determination of three-dimensional structure is a powerful means to facilitate functional characterization, X-ray crystallography has been used to accomplish this task. Here, the expression, purification, crystallization and preliminary crystallographic analysis of HMO2 from S. cerevisiae are reported. The crystal belonged to space group P222, with unit-cell parameters a = 39.35, b = 75.69, c = 108.03?Å, and diffracted to a resolution of 3.0?Å. The crystals are most likely to contain one molecule in the asymmetric unit, with a VM value of 3.19?Å(3)?Da(-1).

SUBMITTER: Guo Z 

PROVIDER: S-EPMC3943102 | biostudies-literature | 2014 Jan

REPOSITORIES: biostudies-literature