Two-Dimensional Crystallisation of Membrane Proteins and Structural Assessment

Fotiadis, Dimitrios José; Engel, Andreas (2015). Two-Dimensional Crystallisation of Membrane Proteins and Structural Assessment. In: eLS (pp. 1-10). John Wiley & Sons, Ltd.

Text Fotiadis Two-Dimensional Crystallisation.pdf - Published Version Restricted to registered users only Available under License Publisher holds Copyright. Download (5MB)

Two-dimensional (2D) crystallisation of Membrane proteins reconstitutes them into their native environment, the lipid bilayer. Electron crystallography
allows the structural analysis of these regular protein–lipid arrays up to atomic resolution. The crystal quality depends on the protein purity, ist stability and on the crystallisation conditions. The basics of 2D crystallisation and different recent advances are reviewed and electron crystallography approaches summarised. Progress in 2D crystallisation, sample preparation, image detectors and automation of the data acquisition and processing pipeline makes 2D electron crystallography particularly attractive for the structural analysis
of membrane proteins that are too small for single-particle analyses and too unstable to form three-dimensional (3D) crystals.

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