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Crystallization, data collection and phasing of the molybdate-binding protein of the phytopathogenXanthomonas axonopodispv.citri

Authors :
Luís Carlos de Souza Ferreira
C. P. Santacruz
J. A. R. G. Barbosa
Andrea Balan
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.

Details

ISSN :
17443091
Volume :
62
Database :
OpenAIRE
Journal :
Acta Crystallographica Section F Structural Biology and Crystallization Communications
Accession number :
edsair.doi.dedup.....3e69e13e571062696e888951f1d9574e