Help Privacy Policy Disclaimer
  Advanced SearchBrowse




Journal Article

Electron microscopy and image analysis of the multicatalytic proteinase

There are no MPG-Authors in the publication available
External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available

Baumeister, W., Dahlmann, B., Hegerl, R., Kopp, F., Kühn, L., & Pfeifer, G. (1988). Electron microscopy and image analysis of the multicatalytic proteinase. FEBS Letters., 241(1-2), 239-245.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0010-74AA-E
One electron micrographs, negatively stained multicatalytic proteinase molecules are viewed end-on (ring shaped) or side-on (rectangular shaped). For aurothioglucose, ammonium molybdate- and phosphotungstate-stained molecules, the dimensions measured are consistent. In contrast, uranyl acetate-staining reveals ring-shaped particles which vary in diameter between 12 and 16 nm. This is due to a partial collapse and substantial flattening of the structure. Digital image analysis of side-on views of the particles reveals a tripartite, reel-shaped structure. Within the ring-like, end-on projections of ammonium molybdate-stained molecules six local centres of mass can be discerned; their position appears to depart, however, from a true six-fold symmetry.