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 A resolution at a synchrotron source. The space group was P3(1)21 or P3(2)21 and the unit-cell parameters were a = b = 126.7, c = 96.0 A.
Hauk
Pricila
P
Centro de Biotecnologia, Instituto Butantan, São Paulo-SP, Brazil.
Guzzo
Cristiane R
CR
Ho
Paulo L
PL
Farah
Chuck S
CS
D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D007921:Leptospira interrogans / Q000737:chemistry* / Q000145:classification*; D008074:Lipoproteins / Q000737:chemistry*
D001425:Bacterial Outer Membrane Proteins; C406589:LipL32 protein, Leptospira; D008074:Lipoproteins