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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.

Original publication




Journal article


Acta Crystallogr D Biol Crystallogr

Publication Date





936 - 938


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