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Journal Article

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

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Dietrich,  Jens
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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Citation

Lebeau, L., Lach, F., Vénien-Bryan, C., Renault, A., Dietrich, J., Jahn, T., et al. (2001). Two-dimensional crystallization of a membrane protein on a detergent-resistant lipid monolayer. Journal of Molecular Biology (London), 308(4), 639-647. doi:10.1006/jmbi.2001.4629.


Cite as: https://hdl.handle.net/21.11116/0000-0007-4439-D
Abstract
wo-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 μm or more. Image processing yielded a projection map at 9 Å resolution, showing three well-separated domains of the membrane-embedded proton ATPase.