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Updated: Apr 12, 2026

Assessing Two-dimensional Crystallization Trials of Small Membrane Proteins for Structural Biology Studies by Electron Crystallography
Published on: October 29, 2010
Inducing two-dimensional crystallization of membrane proteins by dialysis for electron crystallography
Yusuf M Uddin1, Ingeborg Schmidt-Krey2
1School of Biology, Georgia Institute of Technology, Atlanta, Georgia, USA.
Abstract:
Electron crystallography is an electron cryo-microscopy (cryo-EM) method that is particularly suitable for structure-function studies of small membrane proteins, which are crystallized in two-dimensional (2D) arrays for subsequent cryo-EM data collection and image processing. This approach allows for structural analysis of membrane proteins in a close-to-native, phospholipid bilayer environment. The process of growing 2D crystals from purified membrane proteins by dialysis detergent removal is described in this chapter. A short section covers screening for and identifying 2D crystals by transmission electron microscopy, and in the last section, optimization of the purification to obtain crystals of higher quality is discussed.
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