Crystallization and preliminary X-ray analyses of catabolite control protein A, free and in complex with its DNA-binding site

被引：3
|
作者：
Tebbe, J
Orth, P
Küster-Schöck, E
Hillen, W
Saenger, W
Hinrichs, W
机构：
[1] Free Univ Berlin, Inst Kristallog, D-14195 Berlin, Germany
[2] Univ Erlangen Nurnberg, Lehrstuhl Mikrobiol, Inst Mikrobiol Biochem & Genet, D-91058 Erlangen, Germany
来源：
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2000年 / 56卷
关键词：
D O I：
10.1107/S0907444999013104
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
The catabolite control protein (CcpA) from Bacillus megaterium is a member of the bacterial repressor protein family GalR/LacI. CcpA with an N-terminal His-tag was used for crystallization. Crystals of free CcpA and of CcpA in complex with the putative operator sequence (catabolite responsive elements, CRE) were obtained by vapour-diffusion techniques at 291 K using the hanging-drop method. CcpA crystals grown in the presence of polyethylene glycol 8000 belong to the hexagonal space group P6(1)22 or P6(5)22, with unit-cell parameters a = 74.4, c = 238.8 Angstrom. These crystals diffract X-rays to 2.55 Angstrom resolution and contain one monomer of the homodimeric protein per asymmetric unit. Crystals of the CcpA-CRE complex were obtained with ammonium sulfate as precipitant and belong to the tetragonal space group I4(1)22, with unit-cell parameters a = 125, c = 400 Angstrom and one complex per asymmetric unit. Although these cocrystals grew to a sufficient size, X-ray diffraction was limited to 8 Angstrom resolution.
引用
收藏
页码：67 / 69
页数：3
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