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Solution small‐angle X‐ray scattering studies on myosin with a multiwire area detector
Author(s) -
Faruqi A. R.,
Cross R. A.,
KendrickJones J.
Publication year - 1991
Publication title -
journal of applied crystallography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.429
H-Index - 162
ISSN - 1600-5767
DOI - 10.1107/s002188989100047x
Subject(s) - radius of gyration , myosin , scattering , myosin head , small angle scattering , small angle x ray scattering , radius , folding (dsp implementation) , gyration , molecular physics , cross section (physics) , physics , molecule , kinetic energy , detector , crystallography , small molecule , chemistry , optics , biophysics , polymer , nuclear magnetic resonance , geometry , classical mechanics , biology , myosin light chain kinase , computer security , mathematics , computer science , engineering , biochemistry , quantum mechanics , electrical engineering
A point‐focusing small‐angle camera with a multiwire area detector is described along with its application in the study of the conformations of the myosin molecule. Myosin is one of the main contractile proteins, which, in smooth muscle and non‐muscle cells, adopts a number of different conformations: for example an unfolded (6 S ) form which is capable of forming filaments and generating force and a `folded' (10 S ) form, which is most probably a storage form incapable of forming filaments. One of the aims of these solution scattering measurements is to confirm electron microscopic results under more `physiological' conditions and to explore the possibilities of doing kinetic measurements on the transition between the two states. Small‐angle scattering from myosin molecules shows that the radius of gyration of cross section of the 10 S form is greater than for the 6 S form, presumably due to the folding up of the tail part of the molecule. Comparison of the scattering data with model structures shows very good fits for the 6 S form of myosin when both S1 heads are assumed to be close together.