On 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. © 1988.
Baumeister, W., Dahlmann, B., Hegerl, R., Kopp, F., Kuehn, L., & Pfeifer, G. (1988). Electron microscopy and image analysis of the multicatalytic proteinase. FEBS Letters, 241(1–2), 239–245. https://doi.org/10.1016/0014-5793(88)81069-X