Structure of myosin subfragment 1 from low-angle X-ray scattering.
The X-ray scattering pattern produced by a solution of myosin subfragment 1 has been measured to a resolution (Bragg spacing) of 2 nm. We find that for subfragment 1 (S1) prepared by limited papain digestion in the presence of ethylenediaminetetraacetate the radius of gyration is 3.28 +/- 0.06 nm, the volume is 151 +/- 6 nm3, the surface area is 330 +/- 15 nm2, and the length of the maximum chord is 12.0 +/- 1.0 nm. The theoretical scattering patterns from several objects of uniform electron density have been calculated and compared with the observed scattering produced by S1. The recent three-dimensional electron micrograph reconstruction of S1-decorated actin by J. Seymour and E. O'Brien (private communication) generated the calculated pattern that best fit the observed scattering. This fit strongly suggests that this reconstruction resembles subfragment 1. The good correspondence between an S1 structure derived when S1 is attached to actin and a study of free S1 in solution strongly suggests that binding to actin does not grossly distort the shape of S1. This is consistent with the notion that S1 changes its orientation on actin, rather than its shape, in order to generate the contractile force in muscle.
D000818:Animals; D004492:Edetic Acid; D046911:Macromolecular Substances; D008433:Mathematics; D008954:Models, Biological; D008958:Models, Molecular; D009132:Muscles / Q000032:analysis; D009218:Myosins; D010206:Papain; D011487:Protein Conformation; D011817:Rabbits; D012542:Scattering, Radiation; D014961:X-Ray Diffraction
D046911:Macromolecular Substances; D004492:Edetic Acid; D010206:Papain; D009218:Myosins