Configurations of Myosin Heads in the Crab Striated Muscle as Studied by X-Ray Diffraction

  • Katsuzo Wakabayashi
  • Keiichi Namba
  • Toshio Mitsui
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 37)


The configurations of myosin projections in striated muscles from the marine crab, Portunus trituberculatus were described in the relaxed and rigor states at the full overlap length of the thin and thick filaments. The crystallographic period of the thick filament is 101.5 nm (14.5 nm × 7) and the thick filament has four-fold rotational symmetry. In the relaxed state, the myosin projections sit about 19 nm from the thick filament axis, lying just between the surface of the thick filament backbone and that of the thin filament. They have an elongated structure with the length of 10 nm ~ 12 nm and a maximum axial thickness of about 4 nm. They are tilted axially by 20° ~ 30° to the thick filament axis. The configuration of the resting projections sensitively depends on the ionic strength and pH of the solution.

In the rigor state, myosin heads are bound periodically to the thin filaments (Namba, Wakabayashi & Mitsui, 1980); four myosin heads attach in groups every 38.3 rim to successive actin molecules of each strand of Factin. Most of the bound myosin head is incorporated in the thin filament with the centre of gravity 2.8 nm from the thin filament axis. They are inclined at about 30° to and slewed round the thin filament axis.


Thin Filament Myosin Head Layer Line Thick Filament Rigor State 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Cooke, R. and Franks, K. (1980). All myosin heads form bonds with actin in rigor rabbit skeletal muscle. Biochemistry 19: 2265–2269.PubMedCrossRefGoogle Scholar
  2. Elliott, A. and Offer, G. (1978). Shape and flexibility of the myosin molecule. S. Mol. Biol. 123: 505–519.CrossRefGoogle Scholar
  3. Haselgrove, S.C. and Reedy, M.K. (1979). Modeling rigor cross-bridge pattern in muscle I. 248 K. Wakabayashi et al. Initial studies on the rigor lattice of insect flight muscle. Biophys. J. 24: 713–728.CrossRefGoogle Scholar
  4. Haselgrove, J.C. (1980). A model of myosin crossbridge structure consistent with the low- angle X-ray diffraction pattern of vertebrate muscle. J. Mus. Res. Cell Motil. 1: 177–191.CrossRefGoogle Scholar
  5. Holmes, K.C., Tregear, R.T. and Barrington Leigh, J. (1980). Interpretation of the low-angle X-ray diffraction from insect flight muscle in rigor. Proc. R. Soc. Lond. B207: 13–33.CrossRefGoogle Scholar
  6. Huxley, H.E. and Brown, W. (1967). The low-angle X-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor. J. Mol. Biol. 30: 383–434.PubMedCrossRefGoogle Scholar
  7. Maeda, Y., Matsubara, I. and Yagi, N. (1979). Structural changes in thin filaments of crab striated muscle. J. Mol. Biol. 127: 191–201.PubMedCrossRefGoogle Scholar
  8. Namba, K., Wakabayashi, K. and Mitsui, T. (1979). The structure of thin filaments of crab striated muscle in the rigor state. In: Cross–bridge Mechanism in Muscle Contraction, pp. 4–45–470, ed. Sugi, H. and Pollack, G.H. University of Tokyo Press.Google Scholar
  9. Namba, K., Wakabayashi, K. and Mitsui, T. (1980). X-ray structure analysis of the thin filament of crab striated muscle in the rigor state. J. Mol. Biol. 138: 1–26.PubMedCrossRefGoogle Scholar
  10. Offer, G., Couch, J., O’Brien, E. and Elliott, A. (1981). Arrangement of cross-bridges in insect flight muscle in rigor. J. Mol. Biol. 151: 663–702.PubMedCrossRefGoogle Scholar
  11. Reedy, M.K., Holmes, K.C. and Tregear, R.T. (1965). Induced changes in orientation of the crossbridges of glycerinated insect flight muscle. Nature 207: 1276–1280.PubMedCrossRefGoogle Scholar
  12. Squire, J.M. (1972). General model of myosin filament structure II. Myosin filaments and cross-bridge interactions in vertebrate striated and insect flight muscles. J. Mol. Biol. 72: 125–138.PubMedCrossRefGoogle Scholar
  13. Squire, J.M. (1975). Muscle filament structure and muscle contraction. Ann. Rev. Biophys. Bioeng. 4: 137–163.CrossRefGoogle Scholar
  14. Thomas, D.D. and Cooke, R. (1980). Orientation of spin-labelled myosin heads in glycerinated muscle fibres. Biophys. J. 32: 891–906.Google Scholar
  15. Wakabayashi, K. and Namba, K. (1981). X-ray equatorial analysis of crab striated muscle in the relaxed and rigor states. Biophys. Chem. 14: 111–122.PubMedCrossRefGoogle Scholar
  16. Wray, J.S., Vibert, P.J. and Cohen, C. (1975). Diversity of cross-bridge configurations in invertebrate muscles. Nature 257: 561–564.PubMedCrossRefGoogle Scholar
  17. Wray, J.S., Vibert, P.J. and Cohen, C. (1978). Actin filaments in muscle: pattern of myosin and tropomyosin/troponin attachments. J. Mol. Biol. 124: 501–521.CrossRefGoogle Scholar
  18. Wray, J.S. (1979). Structure of the backbone in myosin filaments of muscle. Nature 277: 3740.CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1984

Authors and Affiliations

  • Katsuzo Wakabayashi
    • 1
  • Keiichi Namba
    • 1
  • Toshio Mitsui
    • 1
  1. 1.Department of Biophysical Engineering, Faculty of Engineering ScienceOsaka UniversityToyonaka, Osaka 560Japan

Personalised recommendations