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Crystallization and preliminary structural studies of the ncd motor domain
Author(s) -
Sablin Elena P.,
Fletterick Robert J.
Publication year - 1995
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340210108
Subject(s) - orthorhombic crystal system , crystallization , crystallography , polyethylene glycol , resolution (logic) , domain (mathematical analysis) , molecule , chemistry , materials science , crystal structure , biochemistry , organic chemistry , computer science , mathematics , mathematical analysis , artificial intelligence
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 Å, b = 122.3 Å, c = 68.0 Å, and there is one ncd molecule per asymmetric unit. The crystals diffract X‐ray to at least 2.3 Å and are appropriate for high‐resolution structure determination. © 1995 Wiley‐Liss, Inc.