Cloning, purification, crystallization and preliminary crystallographic analysis of SecA from Enterococcus faecalis

被引：3
|
作者：
Meining, Winfried [1 ]
Scheuring, Johannes
Fischer, Markus
Weinkauf, Sevil
机构：
[1] Karolinska Inst, Dept Biosci, Ctr Struct Bichem, S-10401 Stockholm, Sweden
[2] Tech Univ Munich, Dept Chem, D-8000 Munich, Germany
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2006年 / 62卷
关键词：
D O I：
10.1107/S1744309106017544
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
The gene coding for SecA from Enterococcus faecalis was cloned and overexpressed in Escherichia coli. In this protein, the lysine at position 6 was replaced by an asparagine in order to reduce sensitivity towards proteases. The modified protein was purified and crystallized. Crystals diffracting to 2.4 angstrom resolution were obtained using the vapour-diffusion technique. The crystals belong to the monoclinic space group C2, with unit-cell parameters a = 203.4, b = 49.8, c = 100.8 angstrom, alpha = gamma = 90.0, beta = 119.1 degrees. A selenomethionine derivative was prepared and is currently being tested in crystallization trials.
引用
收藏
页码：583 / 585
页数：3
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