Related Experiment Video
Updated: Jul 24, 2026

Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases
Published on: November 21, 2010
Two-dimensional crystallogenesis of transmembrane proteins
1LPCC, UMR168-CNRS, Institut Curie-Section de Recherche, 11 rue Pierre et Marie Curie, 75005 Paris, France. gervaise.mosser@lps.ens.fr
Abstract:
Two-dimensional crystallogenesis is a crucial step in the long road that leads to the determination of macromolecules structure via electron crystallography. The necessity of having large and highly ordered samples can hold back the resolution of structural works for a long time, and this, despite improvements made in electron microscopes or image processing. Today, finding good conditions for growing two-dimensional crystals still rely on either "biocrystallo-cooks" or on lucky ones. The present review presents the field by first describing the different crystals that one can encounter and the different crystallisation methods used. Then, the effects of different components (such as protein, lipids, detergent, buffer, and temperature) and the different methods (dialysis, hydrophobic adsorption) are discussed. This discussion is punctuated by correspondences made to the world of three-dimensional crystallogenesis. Finally, a guide for setting up 2D crystallogenesis experiments, built on the discussion mentioned before, is proposed to the reader. More than giving recipes, this review is meant to open up the discussions in this field.
Related Concept Videos
Fluid Mosaic Model
Single-pass Transmembrane Proteins
Protein Diffusion in the Membrane
Insertion of Single-pass Transmembrane Proteins in the RER
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Insertion of Multi-pass Transmembrane Proteins in the RER
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
Multi-pass Transmembrane Proteins and β-barrels
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...

