Tomographic 3D reconstruction of quick-frozen, Ca2+ activated insect flight 
muscle

Taylor, Kenneth A.; Schmitz, Holger; Reedy, Mary C.; Goldman, Yale E.; Franzini-Armstrong, Clara; Sasaki, Hiroyuki; Tregear, Richard T.; Poole, Katrina J. V.; Lucaveche, Carmen; Edwards, Robert J.; Chen, Li Fan; Winkler, Hanspeter; Reedy, Michael K.

doi:10.1016/S0092-8674(00)81528-7

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Tomographic 3D reconstruction of quick-frozen, Ca²⁺ activated insect flight muscle

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Poole, Katrina J. V.
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Taylor, K. A., Schmitz, H., Reedy, M. C., Goldman, Y. E., Franzini-Armstrong, C., Sasaki, H., et al. (1999). Tomographic 3D reconstruction of quick-frozen, Ca²⁺ activated insect flight muscle. Cell, 99(4), 421-432. doi:10.1016/S0092-8674(00)81528-7.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-5B2E-6

Abstract

Motor actions of myosin were directly visualized by electron tomography of insect flight muscle quick-frozen during contraction. In 3D images, active crossbridges are usually single myosin heads, bound preferentially to actin target zones sited midway between troponins. Active attached bridges (∼30% of all heads) depart markedly in axial and azimuthal angles from Rayment's rigor acto-S1 model, one-third requiring motor domain (MD) tilting on actin, and two-thirds keeping rigor contact with actin while the light chain domain (LCD) tilts axially from ∼105° to ∼70°. The results suggest the MD tilts and slews on actin from weak to strong binding, followed by swinging of the LCD through an ∼35° axial angle, giving an ∼13 nm interaction distance and an ∼4–6 nm working stroke.