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

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


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Outer Membrane Proteins / chemistry*
  • Crystallization
  • Crystallography, X-Ray
  • Leptospira interrogans / chemistry*
  • Leptospira interrogans / classification*
  • Lipoproteins / chemistry*


  • Bacterial Outer Membrane Proteins
  • LipL32 protein, Leptospira
  • Lipoproteins