Crystallization and preliminary X-ray analysis of an alditol oxidase from Streptomyces coelicolor A3(2)
- Department of Genetics and Microbiology, University of Pavia, Via Ferrata 1, 27100 Pavia (Italy)
- Laboratory of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG (Netherlands)
Alditol oxidase oxidizes a range of alditols into the corresponding aldoses and is an interesting candidate for biotechnological applications. Crystals of alditol oxidase from S. coelicolor A3(2) were obtained by the hanging-drop vapour-diffusion method and diffracted to 1.1 Å resolution. Alditol oxidase is a 45 kDa enzyme containing a covalently bound FAD cofactor. This oxidase efficiently oxidizes a range of alditols to the corresponding aldoses. Owing to its substrate range and regioselectivity, this enzyme is an interesting candidate for biotechnological applications. Crystals of alditol oxidase from Streptomyces coelicolor A3(2) were obtained by the hanging-drop vapour-diffusion method and diffracted to 1.1 Å resolution. The crystals belong to space group C2, with unit-cell parameters a = 107, b = 68, c = 58 Å, β = 94°. Crystals of seleno-l-methionine-labelled alditol oxidase were obtained after seeding the crystallization drops with native microcrystals and showed a diffraction limit of 2.4 Å.
- OSTI ID:
- 22356404
- Journal Information:
- Acta Crystallographica. Section F, Vol. 62, Issue Pt 12; Other Information: PMCID: PMC2225352; PMID: 17142922; PUBLISHER-ID: bo5012; OAI: oai:pubmedcentral.nih.gov:2225352; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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