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 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.
Kang
Gil Bu
GB
Department of Life Science, Kwangju Institute of Science and Technology (K-JIST), Gwangju 500-712, Korea.
Kim
Yun Sik
YS
Im
Young Jun
YJ
Rho
Seong-Hwan
SH
Eom
Soo Hyun
SH
D019732:Amide Synthases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D003627:Data Interpretation, Statistical; D004926:Escherichia coli / Q000235:genetics; D015971:Gene Expression Regulation, Enzymologic; D016480:Helicobacter pylori / Q000201:enzymology*; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification
D011994:Recombinant Proteins; D019732:Amide Synthases; C038479:NAD+ synthase