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Structure of clathrin-coated vesicles from contrast-variation small-angle neutron scattering data

  • J. Skov Pedersen
Conference paper
Part of the Progress in Colloid & Polymer Science book series (PROGCOLLOID, volume 93)

Abstract

Previously published small-angle neutron scattering data from clathrin-coated vesicles have been analyzed in terms of a structural model. The data consist of contrast variation measurements at three different D2O solvent concentrations. 0%, 42%, and 75%. The model used for interpreting the data has spherical symmetry and explicitly takes into account polydispersity, which is described by a Gaussian distribution. A constant thickness of the clathrin coats is assumed. The fitting of the model shows that the coated vesicles consist of a low-density outer protein shell (clathrin) and a central protein shell (accessory polypeptides and receptors) of approximately six times higher denisty. The polydispersity of the samples is about 90 Å (full-width-at-half-maximum value) and the average outer radius is approximately 400 Å. The inner high-density shell has an inner and outer radius of 115 and 190 Å, respectively. A simultaneous fit to the three neutron contrast variation dat sets identifies the lipid membrane with a thickness of 40 Å and an outer radius of 196 Å. The molecular mass of the average particle is 27 × 106 Da. The coated vesicles consist, on average, of approximately 85% protein and 15% lipids. About 40% of the protein mass is situated in the central high-density shell which gives a large amount of protein in the lipid membrane. The densities of the central shell and the lipid membrane show that they hydration is small in the central region.

Key words

Small-angle neutron scattering contrast variation clathrin vesicles molecular structure 

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Copyright information

© Dr. Dietrich Steinkopff Verlag GmbH & Co. KG 1993

Authors and Affiliations

  • J. Skov Pedersen
    • 1
  1. 1.Department of Solid State PhysicsRisó National LaboratoryRoskildeDenmark

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