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 precipitant. 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 = 110.0 degrees.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amide Synthases / chemistry*
-
Amide Synthases / genetics
-
Amide Synthases / isolation & purification
-
Cloning, Molecular
-
Crystallization
-
Crystallography, X-Ray / methods
-
Data Interpretation, Statistical
-
Escherichia coli / genetics
-
Gene Expression Regulation, Enzymologic
-
Helicobacter pylori / enzymology*
-
Recombinant Proteins / chemistry
-
Recombinant Proteins / isolation & purification
Substances
-
Recombinant Proteins
-
Amide Synthases
-
NAD+ synthase