Electron microscopy and image analysis of the multicatalytic proteinase

FEBS Letters

Hegerl, R.¹  Kuehn, L.²  Pfeifer, G.¹  Dahlmann, B.²  Baumeister, W.¹  Kopp, F.² 

[1] Max-Planck-Institut für Biochemie, D-8033 Martinsried, FRG;Diabetes-Forschungsinstitut an der Unversität Düsseldorf, Auf'm Hennekamp 65, D-4 Düsseldorf 1, FRG

关键词: Electron microscopy;    Image analysis;    Multicatalytic proteinase;    Negative staining;   

DOI  :  10.1016/0014-5793(88)81069-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown