title: Inducing two-dimensional crystallization of membrane proteins by dialysis for electron crystallography.
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.
authors.affiliation: School of Biology, Georgia Institute of Technology, Atlanta, Georgia, USA.
authors.forename: Yusuf M
authors.initials: YM
authors.lastname: Uddin
authors.affiliation: School of Biology, Georgia Institute of Technology, Atlanta, Georgia, USA; School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, Georgia, USA. Electronic address: ingeborg.schmidt-krey@biology.gatech.edu.
authors.forename: Ingeborg
authors.initials: I
authors.lastname: Schmidt-Krey
mesh_terms: D000818:Animals; D020285:Cryoelectron Microscopy / Q000379:methods*; D003460:Crystallization / Q000379:methods*; D003902:Detergents / Q000737:chemistry / Q000302:isolation & purification; D003956:Dialysis / Q000379:methods*; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry*; D046529:Microscopy, Electron, Transmission / Q000379:methods
chemical_list: D003902:Detergents; D008565:Membrane Proteins
keywords: 2D crystallization; Detergent; Dialysis; Electron crystallography; Lipids; Membrane protein