Crystallization and preliminary X-ray crystallographic studies of recombinant human leukotriene A4 hydrolase complexed with bestatin

J Mol Biol. 1994 May 20;238(5):854-6. doi: 10.1006/jmbi.1994.1341.

Abstract

Recombinant human leukotriene A4 hydrolase complexed with bestatin, an inhibitor of metalloprotease, has been crystallized by the hanging drop vapor diffusion method using 0.1 M phosphate buffer (pH 6.5) and 50 to 54% saturated ammonium sulfate. The orthorhombic crystals belong to the space group I222 or I2(1)2(1)2(1) with unit cell dimensions of a = 273.6 A, b = 261.3 A and c = 52.9 A. They diffract beyond 2.5 A resolution and a native data set up to 3 A resolution has been collected on an imaging plate Weissenberg camera using synchrotron radiation.

MeSH terms

  • Amino Acid Sequence
  • Crystallization
  • Crystallography, X-Ray
  • Epoxide Hydrolases / chemistry*
  • Humans
  • Leucine / analogs & derivatives*
  • Leucine / chemistry
  • Molecular Sequence Data
  • Molecular Structure
  • Protease Inhibitors / chemistry*
  • Recombinant Proteins / chemistry

Substances

  • Protease Inhibitors
  • Recombinant Proteins
  • Epoxide Hydrolases
  • Leucine
  • ubenimex
  • leukotriene A4 hydrolase