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PMID: 8094463 Published · ppublish English Journal Article

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

Journal of molecular biology ·Vol. 229 ·No. 3 ·1993-02-05 ·Pages 579-84

Zahn R, Harris JR, Pfeifer G, Plückthun A, Baumeister W

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.

MeSH Terms
Bacterial Proteins/chemistry Chaperonin 60 Crystallization Heat-Shock Proteins/chemistry Microscopy, Electron
Chemicals
Bacterial Proteins Chaperonin 60 Heat-Shock Proteins
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Zahn R
Protein Engineering Group, Max-Planck-Institut für Biochemie Am Klopferspitz, Martinsried, Germany.
Harris J R
Pfeifer G
Plückthun A
Baumeister W
Article Info
Journal
Journal of molecular biology
Abbr.
J Mol Biol
ISSN
0022-2836
Published
1993-02-05
Pages
579-84
Language
English
Region
England
NLM ID
2985088R
Subset
IM
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