Structure-function insights of membrane and soluble proteins revealed by electron crystallography

Methods Mol Biol. 2013:955:519-26. doi: 10.1007/978-1-62703-176-9_27.

Abstract

Electron crystallography is emerging as an important method in solving protein structures. While it has found extensive applications in the understanding of membrane protein structure and function at a wide range of resolutions, from revealing oligomeric arrangements to atomic models, electron crystallography has also provided invaluable information on the soluble α/β-tubulin which could not be obtained by any other method to date. Examples of critical insights from selected structures of membrane proteins as well as α/β-tubulin are described here, demonstrating the vast potential of electron crystallography that is first beginning to unfold.

MeSH terms

  • Adenosine Triphosphatases / chemistry
  • Aquaporins / chemistry
  • Bacteriorhodopsins / chemistry
  • Cryoelectron Microscopy / methods*
  • Crystallography
  • Membrane Proteins / chemistry*
  • Plant Proteins / chemistry
  • Receptors, Nicotinic / chemistry
  • Solubility
  • Structure-Activity Relationship

Substances

  • Aquaporins
  • Membrane Proteins
  • Plant Proteins
  • Receptors, Nicotinic
  • Bacteriorhodopsins
  • Adenosine Triphosphatases