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  Two-dimensional crystals of the molecular chaperone GroEL reveal structural plasticity

Zahn, R., Harris, J. R., Pfeifer, G., Plückthun, A., & Baumeister, W. (1993). Two-dimensional crystals of the molecular chaperone GroEL reveal structural plasticity. Journal of Molecular Biology., 229(3), 579-584.

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Zahn, R., Author
Harris, J. R., Author
Pfeifer, G.1, Author              
Plückthun, A., Author
Baumeister, W.1, Author              
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1External Organizations, ou_persistent22              

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Free keywords: *Bacterial Proteins/ch [Chemistry]; Crystallization; GroEL Protein; *Heat-Shock Proteins/ch [Chemistry]; Microscopy, Electron
 Abstract: For two-dimensional (2-D) crystallization we have purified the molecular chaperone GroEL from Escherichia coli to homogeneity. The final and important step for crystallization in the purification procedure was an ATP-agarose column, on which the spacer between ATP and agarose was attached to C8 of adenine. Using the mica spreading "negative staining-carbon film" procedure and polyethylene glycol as a precipitant, we obtained four different 2-D periodic arrays. Two of them turned out to be true crystals. One crystal has P2 symmetry and lattice constants of a = 24.3 nm and b = 16.9 nm, the other has essentially P4 symmetry and shows smoothly varying local changes in the lattice parameters (a = b = 23 (+/- 1.3) nm). Very striking in the P4 crystal is the departure within each individual GroEL particle from the GroEL-typical seven-fold symmetry, which seems to be required for GroEL to accommodate to a crystal symmetry.

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 Dates: 1993
 Publication Status: Published in print
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 Identifiers: eDoc: 318621
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Title: Journal of Molecular Biology.
Source Genre: Journal
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Pages: - Volume / Issue: 229 (3) Sequence Number: - Start / End Page: 579 - 584 Identifier: -