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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Mar 1;65(Pt 3):307-9. doi: 10.1107/S1744309109005533. Epub 2009 Feb 26.

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

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1
Centro de Biotecnologia, Instituto Butantan, São Paulo-SP, Brazil.

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.

PMID:
19255491
PMCID:
PMC2650462
DOI:
10.1107/S1744309109005533
[Indexed for MEDLINE]
Free PMC Article

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