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Crystallizing membrane proteins using lipidic mesophases

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Show simple item record Caffrey, Martin Cherezov, Vadim 2012-07-25T11:27:09Z 2012-07-25T11:27:09Z 2009
dc.description peer-reviewed en_US
dc.description This paper was obtained through PEER (Publishing and the Ecology of European Research)
dc.description.abstract A detailed protocol for crystallizing membrane proteins that makes use of lipidic mesophases is described. This has variously been referred to as the lipid cubic phase or in meso method. The method has been shown to be quite general in that it has been used to solve X-ray crystallographic structures of prokaryotic and eukaryotic proteins, proteins that are monomeric, homo- and hetero-multimeric, chromophore-containing and chromophore-free, and α-helical and β-barrel proteins. Its most recent successes are the human engineered β2-adrenergic and adenosine A2A G protein-coupled receptors. Protocols are provided for preparing and characterizing the lipidic mesophase, for reconstituting the protein into the monoolein-based mesophase, for functional assay of the protein in the mesophase, and for setting up crystallizations in manual mode. Methods for harvesting micro-crystals are also described. The time required to prepare the protein-loaded mesophase and to set up a crystallization plate manually is about one hour. en_US
dc.language.iso eng en_US
dc.publisher Nature Publishing Group en_US
dc.relation.ispartofseries Nature Protocols;4(5), pp. 706-31
dc.subject thin layer chromotography en_US
dc.subject polarized light microscopy en_US
dc.subject small-angle X-ray scattering en_US
dc.title Crystallizing membrane proteins using lipidic mesophases en_US
dc.type info:eu-repo/semantics/article en_US
dc.type.supercollection all_ul_research en_US
dc.type.supercollection ul_published_reviewed en_US
dc.rights.accessrights info:eu-repo/semantics/openAccess en_US

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