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



ID: 318652.0, MPI für Biochemie / Structural Biology (W. Baumeister)
Capsids of tricorn protease studied by electron cryomicroscopy
Authors:Walz, J.; Koster, A. J.; Tamura, T.; Baumeister, W.
Date of Publication (YYYY-MM-DD):1999
Title of Journal:Journal of Structural Biology
Journal Abbrev.:J. Struct. Biol
Volume:128
Issue / Number:1
Start Page:65
End Page:68
Audience:Not Specified
Abstract / Description: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]
Free Keywords:Electron microscopy; Icosahedral capsids; Image analysis; Thermoplasma.; Degradation; Microscopy; Resolution; Products.; Biochemistry & Biophysics in Current Contents(R)/Life Sciences.
External Publication Status:published
Document Type:Article
Communicated by:Anton Hillebrand
Affiliations:MPI für Biochemie/Structural Biology (W. Baumeister)/
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