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Some years ago Reedy, Holmes, and Tregear (1965) noted that ATP had a dramatic effect upon the low-angle X-ray diffraction pattern of gly-cerinated fibers of the flight muscle from the giant water bug Lethocerus maximus. A strong meridional reflection appeared at a spacing of 145 A in the presence of ATP. When the ATP was washed out, this reflection disappeared and its place was taken by a 380 A layer line. With the help of electron microscopy these changes were shown to be due to an alteration in the orientation of the cross-bridges. In the absence of ATP (rigor state) the cross-bridges are at 45° to the filaments. In the presence of ATP the bridges appear to be free from the actin and are right-angled to the thick (myosin) filament (Fig. 1).
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J. Barrington Leigh
University of Alberta
Kenneth C. Holmes
Massachusetts Eye and Ear Infirmary
Hans Georg Mannherz
St. Josef-Hospital
Cold Spring Harbor Symposia on Quantitative Biology
Max Planck Institute for Medical Research
Max Planck Institute of Experimental Medicine
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Leigh et al. (Mon,) studied this question.
synapsesocial.com/papers/6a22fddbc650520b07cb1fd3 — DOI: https://doi.org/10.1101/sqb.1973.037.01.055
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