Preliminary X-ray crystallographic study of the proteasome from Thermoplasma 
acidophilum

Jap, B.; Pühler, G.; Lücke, H.; Typke, D.; Löwe, J.; Stock, D.; Huber, R.; Baumeister, W.

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

Preliminary X-ray crystallographic study of the proteasome from Thermoplasma acidophilum

MPS-Authors

There are no MPG-Authors in the publication available

External Resource

No external resources are shared

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

Jap, B., Pühler, G., Lücke, H., Typke, D., Löwe, J., Stock, D., et al. (1993). Preliminary X-ray crystallographic study of the proteasome from Thermoplasma acidophilum. Journal of Molecular Biology., 234(3), 881-884.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0010-73C5-7

Abstract

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.