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. 2000 Feb 21;148(4):653–664. doi: 10.1083/jcb.148.4.653

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© 2000 The Rockefeller University Press

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

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Electron micrographs of myosin filaments assembled with the 38k protein. In the absence of the 38k protein, unphosphorylated myosin (0.2 μM) did not form filaments (a). However, they were formed from phosphorylated myosin in the absence of the 38k protein (b). Unphosphorylated myosin (0.2 μM) was assembled by 0.55 μM of the 38k protein (c). Filaments formed by 0.2 μM unphosphorylated myosin with 0.69 μM telokin (d). Length distribution of filaments formed by 0.2 μM unphosphorylated myosin with 0.55 μM of the 38k protein (e) and that of filaments formed from phosphorylated myosin in the absence of the 38k protein (f). These histograms were obtained by measurement of the length of 150 filaments. Arrows in e and f indicate average length.