Crystallization and preliminary X-ray diffraction analysis of three EGF domains of EMR2, a 7TM immune-system molecule

Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):936-8. doi: 10.1107/S0907444904005098. Epub 2004 Apr 21.

Abstract

Crystals of three epidermal growth-factor-like (EGF) domains of EMR2 (143 residues) have been grown. EMR2 is a member of the EGF-TM7 family of proteins. Different splice variants exist with between three and five consecutive EGF modules linked to a seven-span transmembrane G-protein-coupled receptor. Although its precise function is unknown, EMR2 is highly expressed in immune tissues and has been shown to weakly bind CD55, a complement-system regulator. Here, crystallization of EMR2 in the presence of Ca(2+), Ba(2+) and Sr(2+) ions is reported. A complete data set has been collected from all three crystal types, all of which belong to space group P2(1). An anomalous Patterson map from the Ba(2+) crystal data reveals three Ba(2+) ions bound within the asymmetric unit.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Barium / chemistry
  • Barium / metabolism
  • Calcium / chemistry
  • Calcium / metabolism
  • Crystallization
  • Crystallography, X-Ray
  • Epidermal Growth Factor / chemistry*
  • Epidermal Growth Factor / metabolism
  • Immune System / chemistry
  • Protein Structure, Tertiary
  • Receptors, G-Protein-Coupled
  • Strontium / chemistry
  • Strontium / metabolism

Substances

  • ADGRE2 protein, human
  • Receptors, G-Protein-Coupled
  • Barium
  • Epidermal Growth Factor
  • Calcium
  • Strontium