Crystallization And X-Ray Analysis Of Nh3- Dependent Nad+ Synthetase From Helicobacter Pylori

Gil   Bu   Kang; Yun   Sik   Kim; Young   Jun   Im; Seong-Hwan      Rho; Soo   Hyun   Eom

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 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

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Protein & Peptide Letters

Title: Crystallization And X-Ray Analysis Of Nh3- Dependent Nad+ Synthetase From Helicobacter Pylori

Volume: 10 Issue: 4

Author(s): Gil Bu Kang, Yun Sik Kim, Young Jun Im, Seong-Hwan Rho and Soo Hyun Eom

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Keywords: amidotransferase, helicobacter pylori, synthetase

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 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°.

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Kang Bu Gil, Kim Sik Yun, Im Jun Young, Rho Seong-Hwan and Eom Hyun Soo, Crystallization And X-Ray Analysis Of Nh3- Dependent Nad+ Synthetase From Helicobacter Pylori, Protein & Peptide Letters 2003; 10 (4) . https://dx.doi.org/10.2174/0929866033478843