Summary: Structural studies of the scrapie prion protein by
electron crystallography
Holger Wille*
, Melissa D. Michelitsch
, Vincent Gue´nebaut§¶
, Surachai Supattapone*
**, Ana Serban*,
Fred E. Cohen*§
, David A. Agard§¶
, and Stanley B. Prusiner*§
*Institute for Neurodegenerative Diseases, Departments of Neurology, Cellular and Molecular Pharmacology, §Biochemistry and Biophysics, and
Medicine, and ¶The Howard Hughes Medical Institute, University of California, San Francisco, CA 94143
Contributed by Stanley B. Prusiner, December 27, 2001
Because the insolubility of the scrapie prion protein (PrPSc) has
frustrated structural studies by x-ray crystallography or NMR
spectroscopy, we used electron crystallography to characterize the
structure of two infectious variants of the prion protein. Isomor-
phous two-dimensional crystals of the N-terminally truncated PrPSc
(PrP 27-30) and a miniprion (PrPSc106) were identified by negative
stain electron microscopy. Image processing allowed the extraction

Source: Agard, David - Department of Biochemistry and Biophysics, University of California at San Francisco

Collections: Biotechnology; Biology and Medicine