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Expression, purification, crystallization and preliminary x-ray analysis of the olfactomedin domain from the sea urchin cell-adhesion protein amassin

Academic Article
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Overview

authors

  • Hillier, B. J.
  • Sundaresan, V.
  • Stout, C. David
  • Vacquier, V. D.

publication date

  • January 2006

journal

  • Acta Crystallographica Section F-Structural Biology and Crystallization Communications  Journal

abstract

  • 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.

subject areas

  • Animals
  • Cell Adhesion Molecules
  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli
  • Extracellular Matrix Proteins
  • Glycoproteins
  • Protein Structure, Tertiary
  • Recombinant Proteins
  • Strongylocentrotus purpuratus
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Identity

PubMed Central ID

  • PMC2150939

International Standard Serial Number (ISSN)

  • 1744-3091

Digital Object Identifier (DOI)

  • 10.1107/s1744309105038996

PubMed ID

  • 16511251
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Additional Document Info

start page

  • 16

end page

  • 19

volume

  • 62

issue

  • Pt 1

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