ISSN:
1399-0047
Source:
Crystallography Journals Online : IUCR Backfile Archive 1948-2001
Topics:
Chemistry and Pharmacology
,
Geosciences
,
Physics
Notes:
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 Å, β = 100.5° and the crystals diffract to 2.7 Å resolution. There are eight monomers in the asymmetric unit giving a VM = 2.6 Å3 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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1107/S0907444995013965
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