Crystallization and X-ray analysis of NH3-dependent NAD+ synthetase from Helicobacter pylori

被引：1
|
作者：
Kang, GB [1 ]
Kim, YS [1 ]
Im, YJ [1 ]
Rho, SH [1 ]
Eom, SH [1 ]
机构：
[1] Kwanju Inst Sci & Technol, Dept Life Sci, Gwangju 500712, South Korea
来源：
PROTEIN AND PEPTIDE LETTERS | 2003年 / 10卷 / 04期
关键词：
amidotransferase; Helicobacter pylori; crystallization; NAD(+) synthetase;
D O I：
10.2174/0929866033478843
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The ubiquitous NAD(+) synthetase catalyzes the key step in the biosynthesis of nicotinamide adenine dinucleotide. NH3-dependent NAD(+) synthetase from Helicobacter pylori was purified to homogeneity and crystallized using PEG 1500 as a preciptant. The crystal diffracted up to a resolution of 2.3+ and was found to belong to space group C2 with unit cell dimensions of a = 93.8, b = 48.3, c = 64.2 A and alpha = gamma = 90, beta = 110.0degrees.
引用
收藏
页码：418 / 421
页数：4
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