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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Crystallization of part of the mitochondrial electron transfer chain: cytochrome c oxidase--cytochrome c complex.

Cytochrome c oxidase (ferrocytochrome c oxygen oxidoreductase, EC 1.9.3.1) was purified from beef heart mitochondria by affinity chromatography. Phospholipids were removed by washing the oxidase with detergent on the affinity column; 1 mole of cardiolipin remained per mole of heme a. The oxidase was mixed with excess cytochrome c in 1.5% (wt/vol) cholate to form a complex. Slow removal of the detergent from the mixture by dialysis resulted in crystallization of cytochrome oxidase in the form of a 1:1 complex with cytochrome c. The chemical composition and spectrophotometric properties of the crystal are described. Increasing the solubility of a hydrophobic membrane protein by combination with hydropholic ligand is demonstrated as a maneuver for crystallizing the membrane protein.[1]

References

  1. Crystallization of part of the mitochondrial electron transfer chain: cytochrome c oxidase--cytochrome c complex. Ozawa, T., Suzuki, H., Tanaka, M. Proc. Natl. Acad. Sci. U.S.A. (1980) [Pubmed]
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