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The arrangement and shape of myosin heads in relaxed muscle have been determined by analysis of low-angle X-ray diffraction data from a very highly ordered vertebrate muscle in bony fish. This reveals the arrangement and interactions between the two heads of the same myosin molecule, the shape of the resting myosin head (M.ADP.Pi) assuming a putative hinge between the myosin catalytic domain and the...
Purpose: To solve the structure of the A-band unit cell in relaxed fish muscle and to use this to follow the molecular movements in active muscle giving regulation and force generation.Methods: Time-resolved X-ray diffraction patterns from contracting plaice fin muscle have been recorded at 1 ms or 5 ms time-intervals (depending on the region being studied) and these are being processed using CCP13...
Using data from fast time-resolved x-ray diffraction experiments on the synchrotrons at Daresbury and (Deutsches Elektronen Synchrotron [DESY]), it is shown that during contraction of fish muscle there are at least two distinct configurations of myosin cross-bridges on actin, that they appear to have different tension producing properties and that they probably differ in the axial tilt of the cross-bridges...
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