Abstract
The structure of the Paired Helical filaments (PHF), a polymer of the microtubule associated protein tau, has been studied by Atomic Force Microscopy (AFM) and by cryoelectron microscopy. Mica and graphite were used as substrates in the AFM analysis with no differences in the results. A banding pattern of 8–12 nm width within the helical structure is found when detailed analysis of the data is performed. High AFM resolution images obtained by using an ultra sharp tip confirm the previous results and suggest that the structures observed are compatible with a helical ribbon made up of two parallel strands. These results were confirmed by cryoelectron microscopy experiments.