Literature DB >> 7716170

Crystallization and preliminary structural studies of the ncd motor domain.

E P Sablin1, R J Fletterick.   

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.

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Year:  1995        PMID： 7716170     DOI： 10.1002/prot.340210108

Source DB:  PubMed          Journal:  Proteins        ISSN： 0887-3585


  4 in total

1.  Polarity of microtubule assemblies during neuronal cell migration.

Authors:  P Rakic; E Knyihar-Csillik; B Csillik
Journal:  Proc Natl Acad Sci U S A       Date:  1996-08-20       Impact factor: 11.205

2.  The shapes of the motor domains of two oppositely directed microtubule motors, ncd and kinesin: a neutron scattering study.

Authors:  S Fujiwara; F J Kull; E P Sablin; D B Stone; R A Mendelson
Journal:  Biophys J       Date:  1995-10       Impact factor: 4.033

3.  A novel adenosine triphosphate analog with a heavy atom to target the nucleotide binding site of proteins.

Authors:  N Naber; M Matuska; E P Sablin; E Pate; R Cooke
Journal:  Protein Sci       Date:  1995-09       Impact factor: 6.725

4.  Nucleotide-dependent movements of the kinesin motor domain predicted by simulated annealing.

Authors:  W Wriggers; K Schulten
Journal:  Biophys J       Date:  1998-08       Impact factor: 4.033
  4 in total

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