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Crystallization, data collection and phasing of the molybdate-binding protein of the phytopathogenXanthomonas axonopodispv.citri
- Source :
- Acta Crystallographica Section F Structural Biology and Crystallization Communications. 62:289-291
- Publication Year :
- 2006
- Publisher :
- International Union of Crystallography (IUCr), 2006.
-
Abstract
- 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.
- Subjects :
- Xanthomonas
Sodium molybdate
Biophysics
Crystal structure
Molybdate
Crystallography, X-Ray
Biochemistry
law.invention
chemistry.chemical_compound
Structural Biology
law
Escherichia coli
Genetics
Crystallization
Molybdenum
Chemistry
Binding protein
Periplasmic space
Condensed Matter Physics
Recombinant Proteins
Crystallography
Crystallization Communications
Periplasmic Binding Proteins
X-ray crystallography
ATP-Binding Cassette Transporters
Orthorhombic crystal system
Subjects
Details
- ISSN :
- 17443091
- Volume :
- 62
- Database :
- OpenAIRE
- Journal :
- Acta Crystallographica Section F Structural Biology and Crystallization Communications
- Accession number :
- edsair.doi.dedup.....3e69e13e571062696e888951f1d9574e