title: Electron and atomic force microscopy of membrane proteins.
abstract: Electron crystallography is becoming a powerful tool for the resolution of membrane protein structures. The past year has seen the production of a bacteriorhodopsin model at 3.5 A and the structure of aquaporin 1 approaching atomic resolution. Determination of surface topographies of 2D crystals using the atomic force microscope is similarly advancing to a level that reveals submolecular details. As the latter is operated in solution, membrane proteins can be observed at work.
authors.affiliation: ME Müller-Institute for Microscopic Structural Biology at the Biozentrum, University of Basel, Switzerland.
authors.forename: J B
authors.initials: JB
authors.lastname: Heymann
authors.forename: D J
authors.initials: DJ
authors.lastname: Müller
authors.forename: K
authors.initials: K
authors.lastname: Mitsuoka
authors.forename: A
authors.initials: A
authors.lastname: Engel
mesh_terms: D051398:Aquaporin 1; D020346:Aquaporins; D001436:Bacteriorhodopsins / Q000648:ultrastructure; D003460:Crystallization; D007473:Ion Channels / Q000648:ultrastructure; D008565:Membrane Proteins / Q000648:ultrastructure*; D018625:Microscopy, Atomic Force / Q000379:methods*; D008854:Microscopy, Electron / Q000379:methods*
chemical_list: D020346:Aquaporins; D007473:Ion Channels; D008565:Membrane Proteins; D051398:Aquaporin 1; D001436:Bacteriorhodopsins