Crystallization and preliminary X-ray diffraction studies of the soluble 14 kDa beta-galactoside-binding lectin from bovine heart

J Mol Biol. 1994 Jan 14;235(2):787-9. doi: 10.1006/jmbi.1994.1034.

Abstract

The soluble 14 kDa beta-galactoside-binding lectin from bovine heart, a member of the S-type lectin family, has been crystallized in a form suitable for X-ray diffraction analysis. The crystals, in the absence of a saccharide ligand, diffract beyond 2.5 A resolution. They are obtained from polyethylene glycol 6000 at pH 6.0. Crystals grow as monoclinic plates, space group P2(1), with cell dimensions: a = 35.47 A, b = 64.33 A, c = 58.78 A and beta = 91.7 degrees. The asymmetric unit contains two molecules related by a 2-fold non-crystallographic axis. Two lectin monomers in the asymmetric unit give a Vm of 2.4 A3/Da, i.e. a solvent content of approximately 50%. The complex of lectin with the saccharide ligand, N-acetyllactosamine, crystallizes in the space group P2(1)2(1)2 with cell dimensions: a = 63.55 A, b = 82.13 A and c = 62.39 A. Crystals of this complex diffract beyond 2.0 A resolution. Two complexes in the asymmetric unit lead to a Vm value of 2.8 A3/Da (57% solvent).

MeSH terms

  • Amino Sugars / chemistry*
  • Animals
  • Cattle
  • Crystallization
  • Crystallography, X-Ray
  • Galectins
  • Hemagglutinins / chemistry*
  • Ligands
  • Muscle Proteins / chemistry*
  • Myocardium / chemistry*

Substances

  • Amino Sugars
  • Galectins
  • Hemagglutinins
  • Ligands
  • Muscle Proteins
  • N-acetyllactosamine