Open AccessCloning, expression, purification, crystallization and preliminary crystallographic analysis of the kinase domain of AtMAP4Kalpha2 from Arabidopsis thaliana
Author(s) -
Shen Liqiang,
Du Xiaoli,
Su Qing,
Li Mingxia,
Zhou Zhiqin
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430911301525x
Subject(s) - arabidopsis thaliana , cloning (programming) , arabidopsis , crystallography , resolution (logic) , domain (mathematical analysis) , crystallization , protein kinase domain , kinase , microbiology and biotechnology , chemistry , protein kinase a , biology , biochemistry , gene , computer science , mathematics , mathematical analysis , organic chemistry , artificial intelligence , mutant , programming language
Arabidopsis thaliana (At) MAP4Kalpha2, a member of the Ste20/PAK‐like protein kinase family, is an essential component of the septum initiation network involved in cell division. To better understand the mode of action of AtMAP4Kalpha2, a structural biology approach has been pursued. In this study, the kinase domain of AtMAP4Kalpha2 was cloned, expressed, purified and crystallized. The crystals diffracted to 1.9 Å resolution and belonged to space group C 222 1 , with unit‐cell parameters a = 55.27, b = 82.93, c = 133.15 Å.