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

页码：418 / 421

页数：4

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