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Updated: Aug 30, 2026

Neutron Crystallography Data Collection and Processing for Modelling Hydrogen Atoms in Protein Structures
Published on: December 1, 2020
Crystallization and X-ray analysis of NH3-dependent NAD+ synthetase from Helicobacter pylori
Gil Bu Kang1, Yun Sik Kim, Young Jun Im
1Department of Life Science, Kwangju Institute of Science and Technology (K-JIST), Gwangju 500-712, Korea.
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.
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