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Small-angle x-ray scattering of human serum high-density lipoproteins.

Small-angle x-ray scattering (SAXRS) studies of the human serum high-density lipoprotein HDL2 indicate a symmetrical particle with a radius of gyration Rg = 46 A. The positions and intensities of subsidiary maxima in the scattering curves are not consistent with those of a uniformly electron dense sphere. Scattering curves calculated for spheres with a step-model radial electron density distribution, show good agreement with the experimental scattering curve for HDL2 only for specific values of the step function used. The dimensions obtained for the electron-deficient core and electron-rich shell model are quantitatively consistent with a predominantly surface location for the HDL2 protein and phospholipid head groups, the more hydrocarbon species being located in the interior of the particle.