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

Abstract

The olfactomedin (OLF) domain from the sea urchin cell-adhesion protein amassin has been crystallized. A native data set extending to 2.7 Å has been collected using an in-house X-ray source. 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.

Authors:
;  [1];  [2]
  1. Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037 (United States)
  2. Center for Marine Biotechnology and Biomedicine, Scripps Institution of Oceanography, University of California San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0202 (United States)
Publication Date:
OSTI Identifier:
22356253
Resource Type:
Journal Article
Journal Name:
Acta Crystallographica. Section F
Additional Journal Information:
Journal Volume: 62; Journal Issue: Pt 1; Other Information: PMCID: PMC2150939; PMID: 16511251; PUBLISHER-ID: za5123; OAI: oai:pubmedcentral.nih.gov:2150939; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; ADHESION; AGGLOMERATION; CRYSTALLIZATION; DISULFIDES; INTERACTIONS; PROTEINS; X-RAY SOURCES

Citation Formats

Hillier, Brian J., E-mail: bhillier@ucsd.edu, Sundaresan, Vidyasankar, Stout, C. David, and Vacquier, Victor D. Expression, purification, crystallization and preliminary X-ray analysis of the olfactomedin domain from the sea urchin cell-adhesion protein amassin. United Kingdom: N. p., 2006. Web. doi:10.1107/S1744309105038996.
Hillier, Brian J., E-mail: bhillier@ucsd.edu, Sundaresan, Vidyasankar, Stout, C. David, & Vacquier, Victor D. Expression, purification, crystallization and preliminary X-ray analysis of the olfactomedin domain from the sea urchin cell-adhesion protein amassin. United Kingdom. https://doi.org/10.1107/S1744309105038996
Hillier, Brian J., E-mail: bhillier@ucsd.edu, Sundaresan, Vidyasankar, Stout, C. David, and Vacquier, Victor D. 2006. "Expression, purification, crystallization and preliminary X-ray analysis of the olfactomedin domain from the sea urchin cell-adhesion protein amassin". United Kingdom. https://doi.org/10.1107/S1744309105038996.
@article{osti_22356253,
title = {Expression, purification, crystallization and preliminary X-ray analysis of the olfactomedin domain from the sea urchin cell-adhesion protein amassin},
author = {Hillier, Brian J., E-mail: bhillier@ucsd.edu and Sundaresan, Vidyasankar and Stout, C. David and Vacquier, Victor D.},
abstractNote = {The olfactomedin (OLF) domain from the sea urchin cell-adhesion protein amassin has been crystallized. A native data set extending to 2.7 Å has been collected using an in-house X-ray source. 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.},
doi = {10.1107/S1744309105038996},
url = {https://www.osti.gov/biblio/22356253}, journal = {Acta Crystallographica. Section F},
issn = {1744-3091},
number = Pt 1,
volume = 62,
place = {United Kingdom},
year = {Sun Jan 01 00:00:00 EST 2006},
month = {Sun Jan 01 00:00:00 EST 2006}
}