Literature DB >> 19255491

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

Pricila Hauk1, Cristiane R Guzzo, Paulo L Ho, Chuck S Farah.   

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.

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Year:  2009        PMID： 19255491      PMCID： PMC2650462          DOI： 10.1107/S1744309109005533

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN： 1744-3091


  18 in total

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