Open AccessCrystallization, data collection and phasing of the molybdate‐binding protein of the phytopathogen Xanthomonas axonopodis pv. citri
Author(s) -
Santacruz C. P.,
Balan A.,
Ferreira L. C. S.,
Barbosa J. A. R. G.
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106003812
Subject(s) - molybdate , crystallization , citrus canker , xanthomonas citri , orthorhombic crystal system , crystallography , molecular replacement , periplasmic space , chemistry , crystal structure , materials science , biology , biochemistry , inorganic chemistry , escherichia coli , bacteria , organic chemistry , gene , genetics
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 Å using synchrotron radiation. The crystal belongs to the orthorhombic space group C 222 1 , with unit‐cell parameters a = 68.15, b = 172.14, c = 112.04 Å. The crystal structure was solved by molecular‐replacement methods and structure refinement is in progress.