Cloning, purification and crystallization of Bacillus anthracis class C acid phosphatase
- Department of Chemistry, University of Missouri-Columbia, Columbia, MO 65211 (United States)
- Department of Veterinary Pathobiology, University of Missouri-Columbia, Columbia, MO 65211 (United States)
Crystallization of a surface-localized acid phosphatase from Bacillus anthracis is reported. Flash annealing increased the high-resolution limit of usable data from 1.8 to 1.6 Å. Cloning, expression, purification and crystallization studies of a recombinant class C acid phosphatase from the Category A pathogen Bacillus anthracis are reported. Large diffraction-quality crystals were grown in the presence of HEPES and Jeffamine ED-2001 at pH 7.0. The crystals belong to space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 53.4, b = 90.1, c = 104.2 Å. The asymmetric unit is predicted to contain two protein molecules with a solvent content of 38%. Two native data sets were collected from the same crystal before and after flash-annealing. The first data set had a mosaicity of 1.6° and a high-resolution limit of 1.8 Å. After flash-annealing, the apparent mosaicity decreased to 0.9° and the high-resolution limit of usable data increased to 1.6 Å. This crystal form is currently being used to determine the structure of B. anthracis class C acid phosphatase with experimental phasing techniques.
- OSTI ID:
- 22360208
- Journal Information:
- Acta Crystallographica. Section F, Vol. 62, Issue Pt 7; Other Information: PMCID: PMC2242959; PMID: 16820700; PUBLISHER-ID: ll5073; OAI: oai:pubmedcentral.nih.gov:2242959; 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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