Expression, purification and crystallization of the catalytic subunit of protein kinase CK2 from Zea mays

被引：27
|
作者：
Guerra, B
Niefind, K
Pinna, LA
Schomburg, D
Issinger, OG
机构：
[1] Odense Univ, Biokem Inst, DK-5230 Odense, Denmark
[2] Univ Cologne, Inst Biochem, D-50674 Cologne, Germany
[3] Univ Padua, Dipartimento Chim Biol, CNR, Target Project ACRO, I-35121 Padua, Italy
[4] Univ Padua, AIRC, I-35121 Padua, Italy
来源：
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1998年 / 54卷
关键词：
D O I：
10.1107/S0907444997010184
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
The catalytic (alpha) subunit of protein kinase CK2 (CK2 alpha) was originally cloned and overexpressed in the Escherichia coli strain pT7-7/BL21(DE3). The protein has been purified to homogeneity and crystallized. The crystals belong to the monoclinic space group CZ, they have unit-cell parameters a = 142.6, b = 61.3, c = 45.6 Angstrom, beta = 103.3 degrees and diffract X-rays to at least 2.0 Angstrom resolution. The calculated crystal packing parameter is V-m = 2.47 Angstrom(3) Da(-1) suggesting that one CK2 alpha molecule is contained in the asymmetric unit and that the solvent content of the unit cell is 50%.
引用
收藏
页码：143 / 145
页数：3
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