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  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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-71A9-8 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-71AA-6
Genre: Journal Article
Alternative Title : J. Struct. Biol

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Walz, J.1, Author              
Koster, A. J.1, Author              
Tamura, T., Author
Baumeister, W.1, Author              
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1External Organizations, escidoc:persistent22              

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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]

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 Dates: 1999
 Publication Status: Published in print
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 Identifiers: eDoc: 318652
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Title: Journal of Structural Biology
  Alternative Title : J. Struct. Biol
Source Genre: Journal
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Pages: - Volume / Issue: 128 (1) Sequence Number: - Start / End Page: 65 - 68 Identifier: -