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Xiao B, Jones D, Madrazo J, et al. Crystallization of a 14-3-3 protein. Acta Crystallogr D Biol Crystallogr. 1996;52:203-6doi: 10.1107/S0907444995009516.
Xiao, B., Jones, D., Madrazo, J., Soneji, Y., Aitken, A., & Gamblin, S. (1996). Crystallization of a 14-3-3 protein. Acta crystallographica. Section D, Biological crystallography, 52203-6. https://doi.org/10.1107/S0907444995009516
Xiao, B, et al. "Crystallization of a 14-3-3 protein." Acta crystallographica. Section D, Biological crystallography vol. 52 (1996): 203-6. doi: https://doi.org/10.1107/S0907444995009516
Xiao B, Jones D, Madrazo J, Soneji Y, Aitken A, Gamblin S. Crystallization of a 14-3-3 protein. Acta Crystallogr D Biol Crystallogr. 1996 Jan 01;52:203-6. doi: 10.1107/S0907444995009516. PMID: 15299747.
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Acta Crystallogr D Biol Crystallogr. 1996 Jan 01;52:203-6. doi: 10.1107/S0907444995009516.

Crystallization of a 14-3-3 protein.

Acta crystallographica. Section D, Biological crystallography

B Xiao, D Jones, J Madrazo, Y Soneji, A Aitken, S Gamblin

Affiliations

  1. Division of Protein Structure, National Institute for Medical Research, London, England.

PMID: 15299747 DOI: 10.1107/S0907444995009516

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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