Purification, crystallization and preliminary X-ray analysis of the M.BseCI DNA methyltransferase from Bacillus stearothermophilus

被引：3
|
作者：
Athanasiadis, A
Papanikolau, Y
Rina, M
Papadovasilaki, M
Dauter, Z
Petratos, K
Bouriotis, V
Kokkinidis, M
机构：
[1] IMBB, GR-71110 IRAKLION, CRETE, GREECE
[2] DESY, EUROPEAN MOL BIOL LAB, D-22603 HAMBURG, GERMANY
来源：
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 1997年 / 53卷
关键词：
D O I：
10.1107/S0907444997002291
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
The DNA methyltransferase M.BseC1 from B. stearothermophilus methylates the N6 atom of the 3' adenine in the sequence 5'-ATCGAT-3'. The 579-residue protein has been isolated and crystallized using seeding and microdialysis techniques. The crystals are monoclinic, space group P2(1) with cell dimensions a = 53.7, b = 85.7, c = 1518 Angstrom and beta = 95.1 degrees, two molecules in the asymmetric unit and diffract to at least 2.5 Angstrom resolution.
引用
收藏
页码：477 / 479
页数：3
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