Crystallization and preliminary X-ray analysis of LipL32 from Leptospira interrogans serovar Copenhageni

LipL32 is a major surface protein that is expressed during infection by pathogenic Leptospira. Here, the crystallization of recombinant LipL32_21-272, which corresponds to the mature LipL32 protein minus its N-terminal lipid-anchored cysteine residue, is described. Selenomethionine-labelled LipL32_21-272 crystals diffracted to 2.25 Å resolution at a synchrotron source. The space group was P3₁21 or P3₂21 and the unit-cell parameters were a = b = 126.7, c = 96.0 Å.