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. 2013 Jul;69(Pt 7):788-91.
doi: 10.1107/S174430911301525X. Epub 2013 Jun 28.

Cloning, expression, purification, crystallization and preliminary crystallographic analysis of the kinase domain of AtMAP4Kalpha2 from Arabidopsis thaliana

Liqiang Shen  1 , Xiaoli Du, Qing Su, Mingxia Li, Zhiqin Zhou
Affiliations

Cloning, expression, purification, crystallization and preliminary crystallographic analysis of the kinase domain of AtMAP4Kalpha2 from Arabidopsis thaliana

Liqiang Shen et al. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jul.

Abstract

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 C2221, with unit-cell parameters a = 55.27, b = 82.93, c = 133.15 Å.

Keywords: Arabidopsis thaliana; AtMAP4Kalpha2.

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Figures

Figure 1
Figure 1
Sequence alignment between AtMAP4Kalpha2-KD and homologous proteins from human and mouse.
Figure 2
Figure 2
AtMAP4Kalpha2-KD (lane 1) was identified by SDS–PAGE. Lane 2 contains molecular-mass markers (labelled in kDa).
Figure 3
Figure 3
(a) Single crystal of AtMAP4Kalpha2-KD. (b) X-ray diffraction image from an AtMAP4Kalpha2-KD crystal. The edge of the diffraction frame is at 1.9 Å resolution.
See this image and copyright information in PMC

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