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Crystallization and preliminary structural studies of the ncd motor domain.

作者信息

Sablin E P, Fletterick R J

机构信息

Department of Biochemistry and Biophysics, University of California at San Francisco 94143-0448, USA.

出版信息

Proteins. 1995 Jan;21(1):68-9. doi: 10.1002/prot.340210108.

DOI:10.1002/prot.340210108
PMID:7716170
Abstract

The motor domain of the kinesin homolog ncd has been crystallized in the presence of MgATP by the vapor diffusion method using polyethylene glycol as the precipitant. The crystals belong to the orthorhombic space group I222 with unit cell dimensions a = 127.1 A, b = 122.3 A, c = 68.0 A, and there is one ncd molecule per asymmetric unit. The crystals diffract X-ray to at least 2.3 A and are appropriate for high-resolution structure determination.

摘要

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