Membrane mimetic systems in CryoEM: keeping membrane proteins in their native environment. (October 2019)

• Record Type: Journal Article
• Authors: Autzen, Henriette E; Julius, David; Cheng, Yifan
• Is Part Of: Current opinion in structural biology. Volume 58(2019)
• Page Start: 259
• Page End: 268
• Publication Date: 2019-10
• Subjects: Molecular biology -- Periodicals; 570
• DOI: 10.1016/j.sbi.2019.05.022
• Languages: English
• ISSNs: 0959-440X

Abstract

Highlights: Single-particle cryoEM facilitates structural determination of membrane proteins without the need of crystallization. Advances in membrane protein sample preparation are facilitating structural studies of membrane proteins. Amphipols have a high affinity for the hydrophobic transmembrane domain and can keep membrane proteins soluble in the absence of free surfactant. Lipid nanodiscs maintain a lipid-like environment for membrane proteins, and facilitate their structural studies by single-particle cryoEM. Styrene-maleic acid copolymers facilitate extraction of membrane proteins in discs consisting of native membrane. Abstract : Advances in electron microscopes, detectors and data processing algorithms have greatly facilitated the structural determination of many challenging integral membrane proteins that have been evasive to crystallization. These breakthroughs facilitate the application and development of various membrane protein solubilization approaches for structural studies, including reconstitution into lipid nanoparticles. In this review, we discuss various approaches for preparing transmembrane proteins for structural determination with single-particle electron cryo microscopy (cryoEM).