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Interactions Between Actin and Myosin Filaments in Skeletal Muscle Visualized in Frozen-Hydrated Thin Sections

B.L. Trus, A.C. Steven, A.W. McDowall, M. Unser, J. Dubochet, R.J. Podolsky

Biophysical Journal, vol. 55, no. 4, pp. 713-724, April 1989.


For the purpose of determining net interactions between actin and myosin filaments in muscle cells, perhaps the single most informative view of the myofilament lattice is its averaged axial projection. We have studied frozen-hydrated transverse thin sections with the goal of obtaining axial projections that are not subject to the limitations of conventional thin sectioning (suspect preservation of native structure) or of equatorial x-ray diffraction analysis (lack of experimental phases). In principle, good preservation of native structure may be achieved with fast freezing, followed by low-dose electron imaging of unstained vitrified cryosections. In practice, however, cryosections undergo large-scale distortions, including irreversible compression; furthermore, phase contrast imaging results in a nonlinear relationship between the projected density of the specimen and the optical density of the micrograph. To overcome these limitations, we have devised methods of image restoration and generalized correlation averaging, and applied them to cryosections of rabbit psoas fibers in both the relaxed and rigor states. Thus visualized, myosin filaments appear thicker than actin filaments by a much smaller margin than in conventional thin sections, and particularly so for rigor muscle. This may result from a significant fraction of the myosin S1-cross-bridges averaging out in projection and thus contributing only to the baseline of projected density. Entering rigor incurs a loss of density from an annulus around the myosin filament, with a compensating accumulation of density around the actin filament. This redistribution of mass represents attachment of the fraction of cross-bridges that are visible above background. Myosin filaments in the "nonoverlap" zone appear to broaden on entering rigor, suggesting that on deprivation of ATP, cross-bridges in situ move outwards even without actin in their immediate proximity.

@ARTICLE(http://bigwww.epfl.ch/publications/trus8901.html,
AUTHOR="Trus, B.L. and Steven, A.C. and McDowall, A.W. and Unser, M.
	and Dubochet, J. and Podolsky, R.J.",
TITLE="Interactions Between Actin and Myosin Filaments in Skeletal
	Muscle Visualized in Frozen-Hydrated Thin Sections",
JOURNAL="Biophysical Journal",
YEAR="1989",
volume="55",
number="4",
pages="713--724",
month="April",
note="")
© 1989 Biophysical Journal. Personal use of this material is permitted. However, permission to reprint/republish this material for advertising or promotional purposes or for creating new collective works for resale or redistribution to servers or lists, or to reuse any copyrighted component of this work in other works must be obtained from Biophysical Journal. This material is presented to ensure timely dissemination of scholarly and technical work. Copyright and all rights therein are retained by authors or by other copyright holders. All persons copying this information are expected to adhere to the terms and constraints invoked by each author's copyright. In most cases, these works may not be reposted without the explicit permission of the copyright holder.
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