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Updated: Jun 23, 2026

Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases

Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases

Published on: November 21, 2010

Crystallizing membrane proteins using lipidic mesophases.

Martin Caffrey¹, Vadim Cherezov

¹Membrane Structural and Functional Biology Group, University of Limerick, Limerick, Ireland. martin.caffrey@ul.ie

Nature Protocols

|April 25, 2009

Summary

This summary is machine-generated.

This study details a versatile lipidic mesophase method for crystallizing membrane proteins. The in meso technique, utilizing lipid cubic phases, has successfully yielded structures of diverse proteins, including G protein-coupled receptors.

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Area of Science:

Structural Biology
Biophysics
Crystallography

Background:

Membrane proteins are crucial for cellular functions but challenging to crystallize.
The lipid cubic phase (in meso) method offers a novel approach for membrane protein crystallization.

Purpose of the Study:

To provide a detailed protocol for crystallizing membrane proteins using the lipid cubic phase method.
To demonstrate the broad applicability of the in meso technique for various protein types.

Main Methods:

Preparation and characterization of lipidic mesophases (lipid cubic phases).
Reconstitution of membrane proteins into monoolein-based mesophases.
Functional assays and crystallization setup in manual mode.
Methods for harvesting microcrystals.

Main Results:

The in meso method is effective for a wide range of proteins: prokaryotic and eukaryotic, monomeric and multimeric, chromophore-containing and -free, alpha-helical and beta-barrel.
Successful crystallization of human beta(2)-adrenergic and adenosine A(2A) G protein-coupled receptors.
The protocol allows for protein-loaded mesophase preparation and crystallization setup within approximately 1 hour.

Conclusions:

The lipid cubic phase (in meso) method is a general and efficient technique for membrane protein crystallization.
This protocol facilitates the structural determination of challenging membrane proteins.
The method has significant implications for understanding membrane protein function and drug discovery.