2h5y | pdb_00002h5y
Crystallographic structure of the Molybdate-Binding Protein of Xanthomonas citri at 1.7 Ang resolution bound to molybdate
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| 2h5y, resolution 1.70Å | |||||||||||||
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| Ligands: | SO4 and MOO | ||||||||||||
| Gene: | modA (Xanthomonas axonopodis pv. citri) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Overview
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.
About this Structure
2H5Y is a Single protein structure of sequence from Xanthomonas axonopodis pv. citri. Full crystallographic information is available from OCA.
Reference
Crystallization, data collection and phasing of the molybdate-binding protein of the phytopathogen Xanthomonas axonopodis pv. citri., Santacruz CP, Balan A, Ferreira LC, Barbosa JA, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Mar 1;62(Pt, 3):289-91. Epub 2006 Feb 24. PMID:16511325
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