Electron and atomic force microscopy of membrane proteins.
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.
Heymann
J B
JB
ME Müller-Institute for Microscopic Structural Biology at the Biozentrum, University of Basel, Switzerland.
Müller
D J
DJ
Mitsuoka
K
K
Engel
A
A
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*
D020346:Aquaporins; D007473:Ion Channels; D008565:Membrane Proteins; D051398:Aquaporin 1; D001436:Bacteriorhodopsins