Generic placeholder image

Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Crystallization And X-Ray Analysis Of Nh3- Dependent Nad+ Synthetase From Helicobacter Pylori

Author(s): Gil Bu Kang, Yun Sik Kim, Young Jun Im, Seong-Hwan Rho and Soo Hyun Eom

Volume 10, Issue 4, 2003

Page: [418 - 421] Pages: 4

DOI: 10.2174/0929866033478843

Price: $65

Abstract

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 Å and α = γ = 90, β = 110.0°.

Keywords: amidotransferase, helicobacter pylori, synthetase


Rights & Permissions Print Cite
© 2024 Bentham Science Publishers | Privacy Policy