Abstract
The program MusLABEL has been devised as a simple aid both in understanding the origin and appearance of fibre diffraction patterns from helical structures and also to simulate the structure and some features of the diffraction patterns from striated muscles and their filament components. Helices are common as preferred conformations in both natural and synthetic macromolecules (e.g. DNA, alpha -helices, polysaccharides, synthetic polymers), and they also occur frequently in extended macromolecular aggregates (e.g. actin filaments, myosin filaments, microtubules, amyloid filaments etc). For this reason, a simple way of visualising the kinds of diffraction patterns that these filament structures can give, particularly for the actin and myosin filaments in muscle, can have educational value and can also be useful as a quick means of evaluating possible symmetries in structural interpretations of diffraction data before embarking on full helical diffraction analysis. A feature of the MusLABEL program is that, when a particular kind of A-band lattice has been set up, for example for vertebrate striated muscle or insect flight muscle, additional parameters can be defined both to describe the limits to the azimuthal and axial ranges over which a myosin head can search for an actin binding site and also to describe the size and position of an actin 'target area' assuming that the azimuthal position of an actin monomer has a large effect in determining whether or not a myosin head can bind to it. By this means the effects of lattice geometry on head attachment can be explored and the diffraction effects of specific labelling patterns on actin can be calculated and simulated. The MusLABEL program, running under Microsoft Windows, is available free on the CCP13 website (www.ccp13.ac.uk) where further documentation is given.
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