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Acta Crystallogr Sect F Struct Biol Cryst Commun
2006 Jan 01;62Pt 1:16-9. doi: 10.1107/S1744309105038996.
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Expression, purification, crystallization and preliminary X-ray analysis of the olfactomedin domain from the sea urchin cell-adhesion protein amassin.
Hillier BJ
,
Sundaresan V
,
Stout CD
,
Vacquier VD
.
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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 A under preliminary cryoconditions, using an in-house generator. This work leads the way to the determination of the first structure of an OLF domain.
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