Crystallization and preliminary crystallographic analysis of decameric and monomeric forms of C49S mutant thioredoxin-dependent AhpC from Helicobacter pylori
- Division of Applied Life Science (BK21 Program), Gyeongsang National University, Jinju 660-701 (Korea, Republic of)
- Department of Microbiology, School of Medicine, Gyeongsang National University, Jinju 660-701 (Korea, Republic of)
Decameric and monomeric forms of recombinant C49S mutant AhpC from H. pylori have been crystallized. Diffraction data were collected to 2.8 and 2.25 Å, respectively. Cys49Ser mutant Helicobacter pylori alkyl hydroperoxide reductase (C49S HpAhpC) was purified under reducing conditions in monomeric and decameric forms. The monomeric form was crystallized by the hanging-drop vapour-diffusion method. The crystals diffracted to 2.25 Å resolution and belonged to space group C2, with unit-cell parameters a = 245.8, b = 140.7, c = 189.5 Å, β = 127°, and contained 20 molecules in the asymmetric unit. A crystal of the decameric form was obtained by the microbatch crystallization method and diffracted to 2.8 Å resolution. It belonged to space group C222, with unit-cell parameters a = 257.5, b = 417.5, c = 95.6 Å. The structure of the monomeric form of C49S HpAhpC has been solved by the molecular-replacement method.
- OSTI ID:
- 22360565
- Journal Information:
- Acta Crystallographica. Section F, Vol. 64, Issue Pt 5; Other Information: PMCID: PMC2376400; PMID: 18475010; PUBLISHER-ID: fw5171; OAI: oai:pubmedcentral.nih.gov:2376400; Copyright (c) International Union of Crystallography 2008; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
Similar Records
Cloning, purification and preliminary X-ray analysis of the C-terminal domain of Helicobacter pylori MotB
Expression, purification, crystallization and preliminary X-ray analysis of an NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from Helicobacter pylori