Open AccessExpression, purification, crystallization and preliminary X‐ray analysis of the olfactomedin domain from the sea urchin cell‐adhesion protein amassin
Author(s) -
Hillier Brian J.,
Sundaresan Vidyasankar,
Stout C. David,
Vacquier Victor D.
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105038996
Subject(s) - sea urchin , strongylocentrotus purpuratus , microbiology and biotechnology , crystallization , heterologous , biology , protein domain , protein family , extracellular , cell adhesion , cell , chemistry , biochemistry , gene , organic chemistry
A family of animal proteins is emerging which contain a conserved protein motif known as an olfactomedin (OLF) domain. Novel extracellular protein–protein interactions occur through this domain. The OLF‐family member amassin, from the sea urchin Strongylocentrotus purpuratus , has previously been identified to mediate a rapid cell‐adhesion event resulting in a large aggregation of coelomocytes, the circulating immune cells. In this work, heterologous expression and purification of the OLF domain from amassin was carried out and initial crystallization trials were performed. A native data set has been collected, extending to 2.7 Å under preliminary cryoconditions, using an in‐house generator. This work leads the way to the determination of the first structure of an OLF domain.