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Crystallization, data collection and data processing of maltose‐binding protein (MalE) from the phytopathogen Xanthomonas axonopodis pv. citri

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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 P6122, 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.
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Keywords: MalE; Xanthomonas axonopodis pv. citri; maltose‐binding proteins

Document Type: Research Article

Publication date: February 1, 2009

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