Crystallization, data collection and phasing of the molybdate-binding protein of the phytopathogen Xanthomonas axonopodis pv. citri.
Xanthomonas axonopodis pv. citri ModA protein is the ABC periplasmic binding component responsible for the capture of molybdate. The protein was crystallized with sodium molybdate using the hanging-drop vapour-diffusion method in the presence of PEG or sulfate. X-ray diffraction data were collected to a maximum resolution of 1.7 A using synchrotron radiation. The crystal belongs to the orthorhombic space group C222(1), with unit-cell parameters a = 68.15, b = 172.14, c = 112.04 A. The crystal structure was solved by molecular-replacement methods and structure refinement is in progress.
Santacruz
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CP
Departamento de Microbiologia, Instituto de Ciências Biomédicas II, Universidade de São Paulo, São Paulo, SP, Brazil.
Balan
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Ferreira
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LC
Barbosa
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JA
D018528:ATP-Binding Cassette Transporters / Q000737:chemistry*; D003460:Crystallization / Q000379:methods; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000378:metabolism; D008982:Molybdenum / Q000378:metabolism*; D033902:Periplasmic Binding Proteins / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry; D014974:Xanthomonas / Q000737:chemistry*
D018528:ATP-Binding Cassette Transporters; D033902:Periplasmic Binding Proteins; D011994:Recombinant Proteins; C044659:molybdate; D008982:Molybdenum