Open AccessCrystallization and preliminary X‐ray diffraction analysis of three EGF domains of EMR2, a 7TM immune‐system molecule
Author(s) -
Abbott Rachel J. M.,
Knott Vroni,
Roversi Pietro,
Neudeck Saskia,
Lukacik Petra,
Handford Penny A.,
Lea Susan M.
Publication year - 2004
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s0907444904005098
Subject(s) - crystallization , epidermal growth factor , transmembrane protein , crystallography , transmembrane domain , regulator , immune system , molecule , chemistry , receptor , function (biology) , ion , biology , microbiology and biotechnology , gene , biochemistry , genetics , organic chemistry
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 P 2 1 . An anomalous Patterson map from the Ba 2+ crystal data reveals three Ba 2+ ions bound within the asymmetric unit.