Crystallization and preliminary X-ray diffraction analysis of three EGF domains of EMR2, a 7TM immune-system molecule.
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.
Abbott
Rachel J M
RJ
Department of Biochemistry, South Parks Road, Oxford OX1 3QU, England.
Knott
Vroni
V
Roversi
Pietro
P
Neudeck
Saskia
S
Lukacik
Petra
P
Handford
Penny A
PA
Lea
Susan M
SM
D000818:Animals; D001464:Barium / Q000737:chemistry / Q000378:metabolism; D002118:Calcium / Q000737:chemistry / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D004815:Epidermal Growth Factor / Q000737:chemistry* / Q000378:metabolism; D007107:Immune System / Q000737:chemistry; D017434:Protein Structure, Tertiary; D043562:Receptors, G-Protein-Coupled; D013324:Strontium / Q000737:chemistry / Q000378:metabolism
C412456:ADGRE2 protein, human; D043562:Receptors, G-Protein-Coupled; D001464:Barium; D004815:Epidermal Growth Factor; D002118:Calcium; D013324:Strontium