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

作者信息

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

机构信息

Protein Engineering Group, Max-Planck-Institut für Biochemie Am Klopferspitz, Martinsried, Germany.

出版信息

J Mol Biol. 1993 Feb 5;229(3):579-84. doi: 10.1006/jmbi.1993.1062.

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.

摘要

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