Crystallization and preliminary x-ray analysis of Escherichia coli GlnK

被引：12

作者：

MacPherson, KHR ^{[1
]}

Xu, YB

Cheah, E

Carr, PD

van Heeswijk, WC

Westerhoff, HV

Luque, E

Vasudevan, SG

Ollis, DL

机构：

[1] Australian Natl Univ, Res Sch Chem, Canberra, ACT 0200, Australia

[2] Free Univ Amsterdam, Fac Biol, Dept Microbial Physiol, NL-1091 HV Amsterdam, Netherlands

[3] James Cook Univ N Queensland, Dept Biochem & Mol Biol, Townsville, Qld 4811, Australia

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1998年 / 54卷

关键词：

D O I：

10.1107/S0907444998001887

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The trimeric sinal-transduction protein GlnK, from Escherichia coli, has been over-expressed, purified to homogeneity and crystallized. The crystals belong to space group P2(1)3 with a = 85.53 Angstrom and have two subunits in the asymmetric unit. The complex of GlnK with ATP crystallized in space group P6(3) with a = 57.45 Angstrom and c = 54.79 Angstrom. These crystals have a single subunit in the asymmetric unit. High-quality diffraction data from crystals of GlnK and the Glnk complex have been collected to 2.0 Angstrom.

引用

页码：996 / 998

页数：3

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