Self-interaction chromatography as a tool for optimizing conditions for membrane protein crystallization

Gabrielsen, M., Nagy, L.A., DeLucas, L.J. and Cogdell, R.J. (2010) Self-interaction chromatography as a tool for optimizing conditions for membrane protein crystallization. Acta Crystallographica. Section D: Biological Crystallography, 66(1), pp. 44-50. (doi: 10.1107/S0907444909043972)

[img] Text


Publisher's URL:


The second virial coefficient, or B value, is a measurement of how well a protein interacts with itself in solution. These interactions can lead to protein crystallization or precipitation, depending on their strength, with a narrow range of B values (the `crystallization slot') being known to promote crystallization. A convenient method of determining the B value is by self-interaction chromatography. This paper describes how the light-harvesting complex 1-reaction centre core complex from Allochromatium vinosum yielded single straight-edged crystals after iterative cycles of self-interaction chromatography and crystallization. This process allowed the rapid screening of small molecules and detergents as crystallization additives. Here, a description is given of how self-interaction chromatography has been utilized to improve the crystallization conditions of a membrane protein.

Item Type:Articles
Keywords:Crystallization, self-interaction chromatography, B values, light-harvesting complex 1, reaction centre
Glasgow Author(s) Enlighten ID:Cogdell, Professor Richard and Gabrielsen, Dr Mads
Authors: Gabrielsen, M., Nagy, L.A., DeLucas, L.J., and Cogdell, R.J.
Subjects:Q Science > QP Physiology
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
Journal Name:Acta Crystallographica. Section D: Biological Crystallography
Publisher:Wiley-Blackwell Publishing, Inc.
ISSN (Online):1399-0047
Copyright Holders:Copyright © 2010 International Union of Crystallography
First Published:First published in Acta Crystallographica Section D: Biological Crystallography 66(1):44-50
Publisher Policy:Reproduced in accordance with the copyright policy of the publisher

University Staff: Request a correction | Enlighten Editors: Update this record