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J Mol Biol. 2001 May 11;308(4):639-47.

Two-dimensional crystallization of a membrane protein on a detergent-resistant lipid monolayer.

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1
Laboratoire de Synthèse Bioorganique associé au CNRS Université Louis Pasteur, Illkirch, 67401, France. lebeau@aspirine.u.strasbg.fr

Abstract

Two-dimensional crystals of a membrane protein, the proton ATPase from plant plasma membranes, have been obtained by a new strategy based on the use of functionalized, fluorinated lipids spread at the air-water interface. Monolayers of the fluorinated lipids are stable even in the presence of high concentrations of various detergents as was established by ellipsometry measurements. A nickel functionalized fluorinated lipid was spread into a monolayer at the air-water interface. The overexpressed His-tagged ATPase solubilized by detergents was added to the subphase. 2D crystals of the membrane protein, embedded in a lipid bilayer, formed as the detergent was removed by adsorption. Electron microscopy indicated that the 2D crystals were single layers with dimensions of 10 microm or more. Image processing yielded a projection map at 9 A resolution, showing three well-separated domains of the membrane-embedded proton ATPase.

PMID:
11350166
DOI:
10.1006/jmbi.2001.4629
[Indexed for MEDLINE]
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