Abstract
An improved negative staining method has been used to visualize monomeric myosin molecules. Each lobe (subfragment 1) of the molecule looked like an elongated pear, and the widths of the thick and thin portions were about 95 and 55 A, respectively. The length of each lobe was about 210 A. It appeared capable of moving azimuthally and altitudinally, utilizing its juncture with the rod portion as the base. The rod portion of the molecule was about 1400 A long and 30 A wide. It also appeared to possess a considerably flexible region at a point about 680 A from the tail-end.
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