Electron and atomic force microscopy of membrane proteins

Heymann, J. B. and Muller, D. J. and Mitsuoka, K. and Engel, A.. (1997) Electron and atomic force microscopy of membrane proteins. Current Opinion in Structural Biology, Vol. 7, H. 4. pp. 543-549.

Full text not available from this repository.

Official URL: http://edoc.unibas.ch/dok/A5257695

Downloads: Statistics Overview


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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology (Engel)
UniBasel Contributors:Engel, Andreas H
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Current Biology
Note:Publication type according to Uni Basel Research Database: Journal article
Last Modified:22 Mar 2012 14:20
Deposited On:22 Mar 2012 13:18

Repository Staff Only: item control page