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• W2208372666 abstract "Two-dimensional (2D) crystals of integral membrane proteins, comprising ordered protein reconstituted into a synthetic lipid bilayer, can be induced to form from detergent solubilized and purified membrane protein sources via the addition of exogenous lipid and the subsequent removal of the solubilizing detergent. This is most commonly accomplished by dialysis of a small volume of ternary protein-detergent-lipid mixture against a large volume of buffer, and can be carried out using common, easily available materials. Following successful crystallization, electron crystallographic data obtained by electron cryo-microscopy (cryo-EM) of vitrified 2D crystals can be used to determine the structure of the lipid bilayer-embedded integral membrane protein." @default.
• W2208372666 created "2016-06-24" @default.
• W2208372666 creator A5048129124 @default.
• W2208372666 creator A5073619140 @default.
• W2208372666 date "2013-01-01" @default.
• W2208372666 modified "2023-09-25" @default.
• W2208372666 title "Two-Dimensional Crystallization by Dialysis for Structural Studies of Membrane Proteins by the Cryo-EM Method Electron Crystallography" @default.
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• W2208372666 doi "https://doi.org/10.1016/b978-0-12-407239-8.00015-x" @default.
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