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Crystallization of a 14-3-3 protein.
Xiao, B; Jones, D; Madrazo, J; Soneji, Y; Aitken, A; Gamblin, S.
  • Xiao B; Division of Protein Structure, National Institute for Medical Research, London, England.
Acta Crystallogr D Biol Crystallogr ; 52(Pt 1): 203-6, 1996 Jan 01.
Article en En | MEDLINE | ID: mdl-15299747
ABSTRACT
Crystals of the tau (tau) isoform of the 14-3-3 family of proteins were grown and shown to belong to the orthorhombic space group P2(1)2(1)2(1) with cell dimensions a = 70.29, b = 79.3, c = 101.00 A. The crystals were needle-like in morphology and less than 10 micro m in two dimensions. Diffraction data were collected using synchrotron radiation sources from flash-cooled crystals. Native data extended to a resolution of 2.6 A and mercury and platinum derivatives diffracted to 3.4 and 3.9 A, respectively. The structure has been solved recently. Here the protein crystallization procedures, the characterization of the crystals and the correlation between crystal habit and diffraction quality are reported.
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Banco de datos: MEDLINE Idioma: En Año: 1996 Tipo del documento: Article
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Banco de datos: MEDLINE Idioma: En Año: 1996 Tipo del documento: Article