Cloning, expression, purification, crystallization and preliminary crystallographic analysis of the kinase domain of AtMAP4Kalpha2 from Arabidopsis thaliana. Issue 7 (22nd July 2013)

• Record Type: Journal Article
• Authors: Shen, Liqiang; Du, Xiaoli; Su, Qing; Li, Mingxia; Zhou, Zhiqin
• Is Part Of: Acta crystallographica. Volume 69:Issue 7(2013:Jul.)
• Page Start: 788
• Page End: 791
• Publication Date: 2013-07-22
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S174430911301525X
• Languages: English
• ISSNs: 1744-3091

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <italic>Arabidopsis thaliana</italic> (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 <italic>C</italic>222₁, with unit‐cell parameters <italic>a</italic> = 55.27, <italic>b</italic> = 82.93, <italic>c</italic> = 133.15 Å.</p> </abstract>