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

✍ Scribed by Gabrielsen, Mads ;Nagy, Lisa A. ;DeLucas, Lawrence J. ;Cogdell, Richard J.

• Publisher: International Union of Crystallography
• Year: 2009
• Tongue: English
• Weight: 503 KB
• Volume: 66
• Category: Article
• ISSN: 0907-4449
• DOI: 10.1107/s0907444909043972

✦ Synopsis

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.