Self-interaction chromatography as a tool for optimizing conditions for membrane protein crystallization.
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.
Gabrielsen
Mads
M
Division of Molecular and Cellular Biology, Faculty of Biological Life Sciences, University of Glasgow, Scotland.
Nagy
Lisa A
LA
DeLucas
Lawrence J
LJ
Cogdell
Richard J
RJ
D001419:Bacteria / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry*; D020134:Catalytic Domain; D011232:Chemical Precipitation; D002846:Chromatography, Affinity; D003460:Crystallization / Q000379:methods*; D018360:Crystallography, X-Ray; D045342:Light-Harvesting Protein Complexes / Q000737:chemistry*; D011485:Protein Binding
D001426:Bacterial Proteins; D045342:Light-Harvesting Protein Complexes