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Electron microscopy and image analysis of the multicatalytic proteinase

Authors :
Baumeister, W.
Dahlmann, B.
Hegerl, R.
Kopp, F.
Kuehn, L.
Pfeifer, G.
Source :
FEBS Letters; January 1988, Vol. 241 Issue: 1 p239-245, 7p
Publication Year :
1988

Abstract

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.

Details

Language :
English
ISSN :
00145793
Volume :
241
Issue :
1
Database :
Supplemental Index
Journal :
FEBS Letters
Publication Type :
Periodical
Accession number :
ejs66309071
Full Text :
https://doi.org/10.1016/0014-5793(88)81069-X