English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Capsids of tricorn protease studied by electron cryomicroscopy

Walz, J., Koster, A. J., Tamura, T., & Baumeister, W. (1999). Capsids of tricorn protease studied by electron cryomicroscopy. Journal of Structural Biology, 128(1), 65-68.

Item is

Basic

show hide
Genre: Journal Article
Alternative Title : J. Struct. Biol

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Walz, J.1, Author           
Koster, A. J.1, Author           
Tamura, T., Author
Baumeister, W.1, Author           
Affiliations:
1External Organizations, ou_persistent22              

Content

show
hide
Free keywords: Electron microscopy; Icosahedral capsids; Image analysis; Thermoplasma.; Degradation; Microscopy; Resolution; Products.; Biochemistry & Biophysics in Current Contents(R)/Life Sciences.
 Abstract: Tricorn protease from the archaeon Thermoplasma acidophilum acts "downstream" of the proteasome; in conjunction with its aminopeptidase cofactors it converts peptides generated by the proteasome into free amino acids. The basic functional unit of Tricorn is a homohexamer of the 121-kDa subunit, 20 of which can assemble further to form an icosahedral capsid with a molecular mass of 14.6 MDa. We have used electron cryomicroscopy to determine the structure of the Tricorn capsids to a resolution of 1.3 nm. (C) 1999 Academic Press. [References: 16]

Details

show
hide
Language(s):
 Dates: 1999
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: eDoc: 318652
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Journal of Structural Biology
  Alternative Title : J. Struct. Biol
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 128 (1) Sequence Number: - Start / End Page: 65 - 68 Identifier: -