Crystallization, data collection and data processing of maltose-binding protein (MalE) from the phytopathogen Xanthomonas axonopodis pv. citri.
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ABSTRACT:
SUBMITTER: Souza CS
PROVIDER: S-EPMC2635876 | biostudies-literature | 2009 Feb
REPOSITORIES: biostudies-literature
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Crystallization, data collection and data processing of maltose-binding protein (MalE) from the phytopathogen Xanthomonas axonopodis pv. citri.
Souza C S CS Ferreira L C S LC Thomas L L Barbosa J A R G JA Balan A A
Acta crystallographica. Section F, Structural biology and crystallization communications 20090107 Pt 2
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 P6(1)22, with unit-cell parameters a = 123.59, b = 123.59, c = 304.20 A, and contained two molecules in the asymetric unit. It diffracted to 2.24 A resolution. ...[more]
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