Open AccessCrystallization, data collection and data processing of maltose‐binding protein (MalE) from the phytopathogen Xanthomonas axonopodis pv. citri
Author(s) -
Souza C. S.,
Ferreira L. C. S.,
Thomas L.,
Barbosa J. A. R. G.,
Balan A.
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108041833
Subject(s) - periplasmic space , maltose , xanthomonas , crystallization , xanthomonas citri , biology , maltose binding protein , chemistry , crystallography , biochemistry , escherichia coli , enzyme , gene , organic chemistry , fusion protein , recombinant dna
Maltose‐binding protein is the periplasmic component of the ABC transporter responsible for the uptake of maltose/maltodextrins. The Xanthomonas axonopodis pv. citri maltose‐binding protein MalE has been crystallized at 293 K using the hanging‐drop vapour‐diffusion method. The crystal belonged to the primitive hexagonal space group P 6 1 22, with unit‐cell parameters a = 123.59, b = 123.59, c = 304.20 Å, and contained two molecules in the asymetric unit. It diffracted to 2.24 Å resolution.