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

ABSTRACT: 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.

SUBMITTER: Hauk P 

PROVIDER: S-EPMC2650462 | biostudies-literature | 2009 Mar

REPOSITORIES: biostudies-literature

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

Hauk Pricila P   Guzzo Cristiane R CR   Ho Paulo L PL   Farah Chuck S CS  

Acta crystallographica. Section F, Structural biology and crystallization communications 20090226 Pt 3

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. ...[more]

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