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

页码：583 / 585

页数：3

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