Regular ArticleThree-Dimensional Reconstruction of Thick Filaments from Rapidly Frozen, Freeze-Substituted Tarantula Muscle
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The myosin interacting-heads motif is present in the relaxed thick filament of the striated muscle of scorpion
2012, Journal of Structural BiologyCitation Excerpt :These results were in general agreement with theoretical models proposed earlier (Squire, 1973). Helical Fourier-based three-dimensional (3D) reconstructions of myosin thick filaments have been calculated for several invertebrates like Limulus (Stewart et al., 1981, 1985), tarantula (Crowther et al., 1985; Padrón et al., 1995), scorpion (Stewart et al., 1985), scallop (Vibert and Craig, 1983) and vertebrates like frog (Stewart and Kensler, 1986). However, these reconstructions of negatively stained thick filaments did not allow unambiguous resolution of the two myosin heads and the myosin subfragment 2 (S2) due to their relatively low (5–7 nm) resolution.
Isolation, electron microscopy and 3D reconstruction of invertebrate muscle myofilaments
2012, MethodsCitation Excerpt :Following freeze-substitution, specimens are embedded and sectioned conventionally. Using this approach, it has been possible to demonstrate the helical organization of myosin heads in thick filaments in situ in tarantula muscle and to determine directly the rotational symmetry of the head organization in both tarantula and scallop muscle by observing thick filaments in transverse section [73–75]. Similar detail has also been observed in vertebrate muscle [76–78] leading to improved insights into vertebrate sarcomeric structure.
Three-Dimensional Reconstruction of Tarantula Myosin Filaments Suggests How Phosphorylation May Regulate Myosin Activity
2008, Journal of Molecular BiologyPurification of native myosin filaments from muscle
2001, Biophysical JournalCitation Excerpt :They are thus appropriate for biochemical, enzymatic, and structural studies. Tarantula muscle was used in this study because of our interest in the molecular organization of the myosin heads in this muscle in the relaxed state and in the structural and biochemical changes that occur in the myosin heads when they are phosphorylated (Crowther et al., 1985; Craig et al., 1987; Padrón et al., 1992, 1995; Offer et al., 2000; Hidalgo et al., 2001). These studies have been hampered by the numerous actin filaments in cryo-electron microscopy (cryo-EM) images of crude filament suspensions (much higher than in specimens examined by negative staining), which interfere greatly with thick filament image analysis.
A new model for the surface arrangement of myosin molecules in tarantula thick filaments
2000, Journal of Molecular Biology