title: Structure-function insights of membrane and soluble proteins revealed by electron crystallography.
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.
authors.affiliation: School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA, USA.
authors.forename: Tina M
authors.initials: TM
authors.lastname: Dreaden
authors.forename: Bharanidharan
authors.initials: B
authors.lastname: Devarajan
authors.forename: Bridgette A
authors.initials: BA
authors.lastname: Barry
authors.forename: Ingeborg
authors.initials: I
authors.lastname: Schmidt-Krey
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry; D020346:Aquaporins / Q000737:chemistry; D001436:Bacteriorhodopsins / Q000737:chemistry; D020285:Cryoelectron Microscopy / Q000379:methods*; D003461:Crystallography; D008565:Membrane Proteins / Q000737:chemistry*; D010940:Plant Proteins / Q000737:chemistry; D011978:Receptors, Nicotinic / Q000737:chemistry; D012995:Solubility; D013329:Structure-Activity Relationship
chemical_list: D020346:Aquaporins; D008565:Membrane Proteins; D010940:Plant Proteins; D011978:Receptors, Nicotinic; D001436:Bacteriorhodopsins; D000251:Adenosine Triphosphatases