The three-dimensional structure of proteasomes from Thermoplasma acidophilum as determined by electron microscopy using random conical tilting

FEBS Lett. 1991 May 20;283(1):117-21. doi: 10.1016/0014-5793(91)80567-m.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cysteine Endopeptidases / chemistry*
  • Cysteine Endopeptidases / ultrastructure
  • Microscopy, Electron
  • Multienzyme Complexes / chemistry*
  • Multienzyme Complexes / ultrastructure
  • Proteasome Endopeptidase Complex
  • Protein Conformation
  • Thermoplasma / enzymology*

Substances

  • Multienzyme Complexes
  • Cysteine Endopeptidases
  • Proteasome Endopeptidase Complex