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Crystallizing membrane proteins using lipidic mesophases
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Journal Article
Crystallizing membrane proteins using lipidic mesophases
2009
Overview
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 β
2
-adrenergic and adenosine A
2A
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 microcrystals are also described. The time required to prepare the protein-loaded mesophase and to set up a crystallization plate manually is about 1 h.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ Bacterial Outer Membrane Proteins - chemistry
/ Biomedical and Life Sciences
/ Computational Biology/Bioinformatics
/ Crystallization - instrumentation
/ Escherichia coli Proteins - chemistry
/ Humans
/ Light-Harvesting Protein Complexes - chemistry
/ Lipids
/ Membrane Proteins - chemistry
/ Membrane Transport Proteins - chemistry
/ Methods
/ Proteins
/ Protocol
/ Receptors, Adrenergic, beta-2 - chemistry
