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

Protein Pept Lett. 2003 Aug;10(4):418-21. doi: 10.2174/0929866033478843.

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