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