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J Struct Biol. 1997 Jun;119(1):28-34.

Crystallization and preliminary X-ray analysis of the single-headed and double-headed motor protein kinesin.

Author information

1
Max-Planck-Unit for Structural Molecular Biology, Hamburg, Germany. frank@unisgil.desy.de

Abstract

Crystals of the single-headed and double-headed kinesin motor domains of Rattus norvegicus have been grown by vapor diffusion using ammonium sulfate as the precipitant. Both crystal systems belong to the orthorhombic space group P2(1)2(1)2(1). Double-headed kinesin crystallized with unit cell constants of a = 72.2 A, b = 91.9 A, and c = 141.7 A, and so far the best crystals diffracted to a maximum resolution of 2.7 A. Using ammonium sulfate single-headed kinesin crystallized in two different crystal forms with cell constants of a = 73.1 A, b = 73.2 A, c = 84.0 A and a = 73.4 A, b = 74.1 A, c = 74.7 A, respectively. They were found to diffract to 2.1 A resolution. Crystals of monomeric kinesin were also obtained with lithium sulfate as precipitant. They have cell constants of a = 71.6 A, b = 73.7 A, and c = 74.1 A and diffract up to 1.7 A resolution.

PMID:
9216086
DOI:
10.1006/jsbi.1997.3872
[Indexed for MEDLINE]

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