Advances in structural and functional analysis of membrane proteins by electron crystallography

Structure. 2011 Oct 12;19(10):1381-93. doi: 10.1016/j.str.2011.09.001.

Abstract

Electron crystallography is a powerful technique for the study of membrane protein structure and function in the lipid environment. When well-ordered two-dimensional crystals are obtained the structure of both protein and lipid can be determined and lipid-protein interactions analyzed. Protons and ionic charges can be visualized by electron crystallography and the protein of interest can be captured for structural analysis in a variety of physiologically distinct states. This review highlights the strengths of electron crystallography and the momentum that is building up in automation and the development of high throughput tools and methods for structural and functional analysis of membrane proteins by electron crystallography.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Aquaporin 1 / chemistry
  • Archaea / chemistry
  • Bacteriorhodopsins / chemistry
  • Cell Membrane / chemistry*
  • Cell Membrane / physiology
  • Cryoelectron Microscopy
  • Crystallography / instrumentation
  • Crystallography / methods*
  • Detergents / chemistry
  • Dialysis / instrumentation
  • Electronic Data Processing
  • Humans
  • Image Processing, Computer-Assisted
  • Lipid Bilayers / chemistry
  • Membrane Proteins / chemistry*
  • Membrane Proteins / physiology
  • Membrane Transport Proteins / chemistry
  • Protein Conformation
  • Static Electricity

Substances

  • AQP1 protein, human
  • Detergents
  • Lipid Bilayers
  • Membrane Proteins
  • Membrane Transport Proteins
  • Aquaporin 1
  • Bacteriorhodopsins