title: Crystallization and preliminary structural studies of the ncd motor domain.
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.
authors.affiliation: Department of Biochemistry and Biophysics, University of California at San Francisco 94143-0448, USA.
authors.forename: E P
authors.initials: EP
authors.lastname: Sablin
authors.forename: R J
authors.initials: RJ
authors.lastname: Fletterick
mesh_terms: D000818:Animals; D003460:Crystallization; D029721:Drosophila Proteins; D016547:Kinesins; D008868:Microtubule Proteins / Q000737:chemistry*; D017433:Protein Structure, Secondary
chemical_list: D029721:Drosophila Proteins; D008868:Microtubule Proteins; C066696:ncd protein, Drosophila; D016547:Kinesins