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

Authors: Abbott, Rachel J. M.; Knott, Vroni; Roversi, Pietro; Neudeck, Saskia; Lukacik, Petra; Handford, Penny A.; Lea, Susan M.

Source: Acta Crystallographica Section D, Volume 60, Number 5, May 2004 , pp. 936-938(3)

Publisher: Blackwell Publishing

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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 Ca²⁺, Ba²⁺ and Sr²⁺ ions is reported. A complete data set has been collected from all three crystal types, all of which belong to space group P2₁. An anomalous Patterson map from the Ba²⁺ crystal data reveals three Ba²⁺ ions bound within the asymmetric unit.

Keywords: EMR2; CD97; CD55; EGF; 7TM

Document Type: Research article

DOI: 10.1107/S0907444904005098

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