Expression, purification, crystallization and preliminary X-ray analysis of YaeQ (XAC2396) from Xanthomonas axonopodis pv. citri
- Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, CEP 05508-000, São Paulo, SP (Brazil)
- Instituto de Física de São Carlos, Universidade de São Paulo, CEP 13560-970, São Carlos, SP (Brazil)
The first crystallographic study of a member of the YaeQ family of proteins, which are conserved in a small group of Gram-negative bacteria, most of which are animal or plant pathogens, is reported. Diffraction data were collected to 1.9 Å resolution and an interpretable electron-density map was obtained. Xanthomonas axonopodis pv. citri YaeQ (XAC2396) is a member of a family of bacterial proteins conserved in several Gram-negative pathogens. Here, the cloning, expression, purification and crystallization of the 182-residue (20.6 kDa) YaeQ protein are described. Recombinant YaeQ containing selenomethionine was crystallized in space group P2{sub 1} and crystals diffracted to 1.9 Å resolution at a synchrotron source. The unit-cell parameters are a = 39.75, b = 91.88, c = 48.03 Å, β = 108.37°. The calculated Matthews coefficient suggests the presence of two YaeQ molecules in the asymmetric unit. Initial experimental phases were calculated by the multiple-wavelength anomalous dispersion technique and an interpretable electron-density map was obtained.
- OSTI ID:
- 22356006
- Journal Information:
- Acta Crystallographica. Section F, Vol. 61, Issue Pt 5; Other Information: PMCID: PMC1952311; PMID: 16511077; PUBLISHER-ID: en5110; OAI: oai:pubmedcentral.nih.gov:1952311; Copyright (c) International Union of Crystallography 2005; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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