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          Institute: MPI für Biochemie     Collection: Structural Biology (W. Baumeister)     Display Documents



ID: 318345.0, MPI für Biochemie / Structural Biology (W. Baumeister)
The three-dimensional structure of proteasomes from Thermoplasma acidophilum as determined by electron microscopy using random conical tilting
Authors:Hegerl, R.; Pfeifer, G.; Pühler, G.; Dahlmann, B.; Baumeister, W.
Date of Publication (YYYY-MM-DD):1991
Title of Journal:FEBS Letters.
Volume:283
Issue / Number:1
Start Page:117
End Page:121
Audience:Not Specified
Abstract / Description:The three-dimensional structure of proteasomes from the archaebacterium Thermoplasma acidophilum has been determined to a resolution of approximately 2 nm from electron micrographs of negatively stained preparations using the method of 'random conical tilting'. The particles turn out to be essentially cylinder-shaped barrels, 15 nm long and 11 nm wide, enclosing a tripartite inner compartiment. An account is given of some of the present limitations which prevent to attain a higher resolution and possible ways to overcome these limitations are indicated.
Free Keywords:*Cysteine Endopeptidases/ch [Chemistry]; Cysteine Endopeptidases/ul [Ultrastructure]; Microscopy, Electron; *Multienzyme Complexes/ch [Chemistry]; Multienzyme Complexes/ul [Ultrastructure]; Protein Conformation; Support, Non-U.S. Gov't; *Thermoplasma/en [Enzymology]
External Publication Status:published
Document Type:Article
Communicated by:Anton Hillebrand
Affiliations:MPI für Biochemie/Structural Biology (W. Baumeister)/
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