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Sebastião P, Dauter Z, Saraiva MJ, et al. Crystallization and preliminary X-ray diffraction studies of Leu55Pro variant transthyretin. Acta Crystallogr D Biol Crystallogr. 1996;52:566-8doi: 10.1107/S0907444995013965.
Sebastião, P., Dauter, Z., Saraiva, M. J., & Damas, A. M. (1996). Crystallization and preliminary X-ray diffraction studies of Leu55Pro variant transthyretin. Acta crystallographica. Section D, Biological crystallography, 52566-8. https://doi.org/10.1107/S0907444995013965
Sebastião, P, et al. "Crystallization and preliminary X-ray diffraction studies of Leu55Pro variant transthyretin." Acta crystallographica. Section D, Biological crystallography vol. 52 (1996): 566-8. doi: https://doi.org/10.1107/S0907444995013965
Sebastião P, Dauter Z, Saraiva MJ, Damas AM. Crystallization and preliminary X-ray diffraction studies of Leu55Pro variant transthyretin. Acta Crystallogr D Biol Crystallogr. 1996 May 01;52:566-8. doi: 10.1107/S0907444995013965. PMID: 15299680.
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Acta Crystallogr D Biol Crystallogr. 1996 May 01;52:566-8. doi: 10.1107/S0907444995013965.

Crystallization and preliminary X-ray diffraction studies of Leu55Pro variant transthyretin.

Acta crystallographica. Section D, Biological crystallography

P Sebastião, Z Dauter, M J Saraiva, A M Damas

Affiliations

  1. Instituto de Ciências Biomédicas de Abel Salazar, Universidade do Porto, Portugal.

PMID: 15299680 DOI: 10.1107/S0907444995013965

Abstract

The amyloidogenic Leu55Pro variant of transthyretin has been expressed, purified and crystallized in space group C2. The cell constants are a = 149.99, b = 78.74, c = 98.95 A, beta = 100.5 degrees and the crystals diffract to 2.7 A resolution. There are eight monomers in the asymmetric unit giving a V(M) = 2.6 A(3) Da(-1) and 53% solvent content. In the wild-type protein, the crystals are orthorhombic with two monomers in the asymmetric unit. The wild-type protein is a tetramer composed of four identical subunits [Blake, Geisow, Oatley, Rerat & Rerat (1978). J. Mol. Biol. 121, 339-356.] and a molecular-replacement solution for the Leu55Pro variant was obtained using one monomer of the wild-type protein as a model. Rigid-body refinement of the eight monomers in the asymmetric unit and subsequent refinement using molecular dynamics were performed with X-PLOR, leading to a current R factor of 20.3% for all the data. The crystallographic packing of the molecules is different from the one presented by the wild-type protein, opening new perspectives for understanding how this protein aggregates to form amyloid fibrils.

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