The Structural Electron Microscopy Team focuses on the use of electron microscopy and image analysis based methods to determine the three-dimensional structure and explain the function of large multi protein complexes. Generally it is difficult to determine the structures of such complexes by standard crystallographic or NMR techniques since they are large and are frequently only available in small amounts and at limited concentrations.
Currently, the main project areas within the team concern the structure of the 26S proteasome and the COP9 signalosome, both of which play central roles in the ubiquitin proteasome system.
The Structural Electron Microscopy Team is also actively involved in collaborative projects with other groups both within and outside the Institute of Cancer Research. These projects include the electron microsope based structural analysis of the anaphase promoting complex (Professor David Barford, Division of Structural Biology) and the minichromosome maintenance complex (Dr John Diffley, London Research Institute).
Structural Electron Microscopy
Structural Electron Microscopy is a technique which is particularly effective in determining the three-dimensional structure of large protein complexes.
Selective protein removal is an essential regulatory mechanism in cellular homeostasis and cell division. The ubiquitin-proteasome system is responsible for the highly regulated targeting and proteolysis of such proteins. The 26S proteasome is a key component of the ubiquitin-proteasome system.