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



ID: 318476.0, MPI für Biochemie / Structural Biology (W. Baumeister)
Preliminary X-ray crystallographic study of the proteasome from Thermoplasma acidophilum
Authors:Jap, B.; Pühler, G.; Lücke, H.; Typke, D.; Löwe, J.; Stock, D.; Huber, R.; Baumeister, W.
Date of Publication (YYYY-MM-DD):1993
Title of Journal:Journal of Molecular Biology.
Volume:234
Issue / Number:3
Start Page:881
End Page:884
Audience:Not Specified
Abstract / Description:Single cystals of proteasomes from the archaebacterium Thermoplasma acidophilum were obtained using the hanging-drop vapor diffusion method. The crystals diffract to better than 3.0 A and belong to the orthorhombic space group P2(1)2(1)2(1) with unit cell dimensions a = 308.9 A, b = 208.8 A and c = 116.9 A. There is one molecular complex in the asymmetric unit. Two potentially useful heavy-atom derivatives have been obtained. The self-rotation function of the native Patterson map shows local sevenfold symmetry, consistent with the low-resolution structure obtained by electron microscopic techniques. The unit cell dimensions and crystal symmetry together with the shape and size of the proteasome suggest a packing arrangement of proteasome molecules in the unit cell, with their cylinder axis nearly parallel to the crystallographic a-axis.
Free Keywords:Crystallization; Crystallography, X-Ray/mt [Methods]; *Cysteine Endopeptidases/ch [Chemistry]; Cysteine Endopeptidases/ip [Isolation & Purification]; *Multienzyme Complexes/ch [Chemistry]; Multienzyme Complexes/ip [Isolation & Purification]; *Protein Conformation; Support, Non-U.S. Gov't; Support, U.S. Gov't, Non-P.H.S.; Support, U.S. Gov't, P.H.S.; *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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