Crystallization And X-Ray Analysis Of Nh3- Dependent Nad+ Synthetase From Helicobacter Pylori
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
Document Type: Review Article
Affiliations: Department of Life Science, Kwangju Institute of Science and Technology (K-JIST), Gwangju 500-712, Korea
Publication date: 01 August 2003
- Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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