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)

Abstract

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
• Status: Published
• Refereed: Yes
• 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 > School of Molecular Biosciences
• Journal Name: Acta Crystallographica. Section D: Biological Crystallography
• Publisher: Wiley-Blackwell Publishing, Inc.
• ISSN: 0907-4449
• 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