Crystallization and preliminary X-ray diffraction analysis of the human dimeric S-Lac lectin (L-14-II)

J Mol Biol. 1993 Oct 5;233(3):553-5. doi: 10.1006/jmbi.1993.1533.

Abstract

The human recombinant S-Lac lectin, L-14-II, produced in an Escherichia coli expression system, has been co-crystallized in the presence of lactose by the hanging drop vapor diffusion method. The crystals grow in space group P2(1)2(1)2(1) with unit cell dimensions of a = 43.6 A, b = 57.8 A, c = 108.2 A, with a dimer in the asymmetric unit. On a conventional rotating anode the crystals diffract to at least 2.8 A resolution.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallography, X-Ray
  • Escherichia coli / genetics
  • Galectins
  • Hemagglutinins / chemistry*
  • Humans
  • Lectins / chemistry*
  • Protein Conformation
  • Recombinant Proteins / chemistry

Substances

  • Galectins
  • Hemagglutinins
  • Lectins
  • Recombinant Proteins