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Refolding of Escherichia coli produced membrane protein inclusion bodies immobilised by nickel chelating chromatography

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Rogl,  Hans
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Kühlbrandt,  Werner
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Collinson,  Ian
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Rogl, H., Kosemund, K., Kühlbrandt, W., & Collinson, I. (1998). Refolding of Escherichia coli produced membrane protein inclusion bodies immobilised by nickel chelating chromatography. FEBS Letters, 432(1-2), 21-26. doi:10.1016/s0014-5793(98)00825-4.


Cite as: http://hdl.handle.net/21.11116/0000-0007-A22E-F
Abstract
Two distinctly different membrane proteins, which produced inclusion bodies in Escherichia coli, have been refolded to reconstitute properties appropriate to their native counterparts. The method employed utilises nickel chelating chromatography, where the solubilised inclusion bodies bind, refold and elute. Our aims were to release a large pool of membrane protein for functional, mutational and crystallisation screening studies. It is hoped that the methods described here will have a general application for other membrane proteins which have formed inclusion bodies.