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人蛋白激酶CK2调节亚基的结晶及初步X射线衍射分析

Crystallization and preliminary x-ray diffraction analysis of the regulatory subunit of human protein kinase CK2.

作者信息

Chantalat L, Leroy D, Filhol O, Quitaine N, Chambaz E M, Cochet C, Dideberg O

机构信息

Laboratoire de Cristallographie Macromoléculaire, Institut de Biologie Structurale Jean-Pierre Ebel, CNRS-CEA, 41 Avenue des Martyrs, 38027 Grenoble CEDEX 1, France.

出版信息

Acta Crystallogr D Biol Crystallogr. 1999 Apr;55(Pt 4):895-7. doi: 10.1107/s0907444998016680.

DOI:10.1107/s0907444998016680
PMID:10089327
Abstract

Protein kinase CK2 is a tetramer composed of two alpha catalytic subunits and two beta regulatory subunits. A C-terminal truncated form of the beta subunit has been overproduced in Escherichia coli and purified to homogeneity. Two crystal forms of the truncated protein which diffract to at least 2 A resolution have been obtained. Form I belongs to the monoclinic space group P21, with unit-cell parameters a = 49.9, b = 92.9, c = 53.7 A, beta = 96.3 degrees, and yields plate-like crystals. Form II belongs to the tetragonal space group P42212, with unit-cell parameters a = 132.19, b = 132.19, c = 63.79 A, and produces rod-shaped crystals. Both crystal forms have a functional dimer in the crystal asymmetric unit.

摘要

蛋白激酶CK2是一种由两个α催化亚基和两个β调节亚基组成的四聚体。β亚基的C末端截短形式已在大肠杆菌中过量表达并纯化至同质。已获得截短蛋白的两种晶体形式,其衍射分辨率至少为2埃。晶型I属于单斜空间群P21,晶胞参数为a = 49.9、b = 92.9、c = 53.7埃,β = 96.3°,并产生片状晶体。晶型II属于四方空间群P42212,晶胞参数为a = 132.19、b = 132.19、c = 63.79埃,并产生棒状晶体。两种晶体形式在晶体不对称单元中均具有功能性二聚体。

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