The MalE protein of Xanthomonas axonopodis pv. Citri belongs to a family of transporters denominated ABC transporters (ATP-Binding Cassete). The mode gene was cloned and expressed in Escherichia coli and the recombinant protein was able to bind maltose in vitro experiments . Three-dimentional structures of maltose/maltotriose transporters have been solved in other species including Escherichia coli K12, Thermococcus litoralis, Alicyclobacillus acidocaldarius and Pyrococcus furiosus, however, no ortholog derived from plant-associated bacteria have been reported so far and the transport of sugars in Xanthomonas is completely unknown. The recombinant purified protein was able to form bipiramidal which have diffracted at low resolution (around 4-10 Å). In this work we report new attempts to crystallization and diffraction. The purified protein was submitted to the crystallization trials with the Jena Biosciences kit, using the hanging drop vapour diffusion method and 10 mg/ml of protein (200 uM) bound to 400 uM maltose at 18°C and 4°C. The crystals were obtained in 12 different conditions and used in the diffraction assays. The best diffraction pattern was obtained for the crystals grown at 17% PEG 4000; 0,1M Tris-HCl pH 8,0; 0,2 M lythium sulfate at 4° C. X-ray diffraction data were collected to a maximum resolution of 3.2 Å using a synchrotron-radiation source. Diffraction data were collected for two different crystals from the same drop and the data processing revealed different space groups for both crystals, P3 and I4. Indeed, the binding of the protein to the different sugars was monitored by circular dichroism analysis.