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Cloning, purification, crystallization and preliminary X‐ray studies of HMO2 from Saccharomyces cerevisiae
Author(s) -
Guo Zhen,
Zhang Shaocheng,
Zhang Hongpeng,
Jin Li,
Zhao Shasha,
Yang Wei,
Tang Jian,
Wang Deqiang
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x13031580
Subject(s) - cloning (programming) , saccharomyces cerevisiae , crystallization , computational biology , genetics , biology , chemistry , yeast , computer science , programming language , organic chemistry
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 P 222, 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 V M value of 3.19 Å 3 Da −1 .