Published July 26, 2008 | Version v1
Journal article

Expression, purification, crystallization and preliminary X-ray analysis of an NAD-dependent glyceraldehyde-3-phosphate dehydrogenase from Helicobacter pylori

  • 1. Henry Wellcome Laboratories for Structural Biology, University of Leicester, Leicester LE1 9HN (United Kingdom)

Description

Glyceraldehyde-3-phosphate dehydrogenase B from H. pylori has been cloned, expressed, purified and crystallized in the presence of NAD. Crystals of GAPDHB diffracted to 2.8 Å resolution and belonged to space group P6522, with unit-cell parameters a = b = 166.1, c = 253.1 Å. Helicobacter pylori is a dangerous human pathogen that resides in the upper gastrointestinal tract. Little is known about its metabolism and with the onset of antibiotic resistance new treatments are required. In this study, the expression, purification, crystallization and preliminary X-ray diffraction of an NAD-dependent glyceraldehyde-3-phosphate dehydrogenase from H. pylori are reported

Availability note (English)

Available from http://dx.doi.org/10.1107/S1744309108020368; Available from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2494976

Additional details

Publishing Information

Journal Title
Acta Crystallographica. Section F
Journal Volume
64
Journal Issue
Pt 8
Journal Page Range
p. 727-729
ISSN
1744-3091
CODEN
ACSFCL

INIS

Country of Publication
United Kingdom
Country of Input or Organization
International Atomic Energy Agency (IAEA)
INIS RN
46065900
Subject category
S75: CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY;
Descriptors DEI
CRYSTALLIZATION; CRYSTALS; PHOSPHATES; RESOLUTION; SPACE GROUPS; X-RAY DIFFRACTION
Descriptors DEC
COHERENT SCATTERING; DIFFRACTION; OXYGEN COMPOUNDS; PHASE TRANSFORMATIONS; PHOSPHORUS COMPOUNDS; SCATTERING; SYMMETRY GROUPS

Optional Information

Copyright
Copyright (c) International Union of Crystallography 2008
Notes
PMCID: PMC2494976; PMID: 18678942; PUBLISHER-ID: nj5012; OAI: oai:pubmedcentral.nih.gov:2494976