Myosin head configuration in relaxed fish muscle: resting state myosin heads must swing axially by up to 150 Å or turn upside down to reach rigor

Hudson, Liam; Harford, Jeffrey J.; Denny, Richard; Squire, John M.

doi:10.1006/jmbi.1997.1321

Cited by 63 publications

(129 citation statements)

References 65 publications

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“…The fish muscle myosin filament model of Hudson et al (1997), based on lowangle X-ray diffraction, included the head perturbations. Therefore, for direct comparison of the X-ray modeling with the helical reconstruction presented here from electron micrographs, we have produced a helical approximation to the X-ray model in which the perturbation has been removed.…”

Section: Resultsmentioning

confidence: 99%

“…One of the problems with simulated annealing parameter searches such as used by Hudson et al (1997) is that they are used because with a reasonable number of parameters (here about 20) the alternative systematic global search method using the whole possible range of each parameter and a reasonably small increment size makes the computation prohibitively long (months to years) even on very fast computers. Simulated annealing methods are much faster and home in on good parameter sets in a relatively short time (hours/ days).…”

Section: Introductionmentioning

confidence: 99%

“…The most complete description to date of the likely disposition of the myosin heads in relaxed vertebrate muscle has been obtained by modeling of the highly sampled low-angle X-ray diffraction pattern from plaice fin muscle (Harford and Squire, 1986;Hudson et al, 1997;Squire et al, 1998). Bony fish muscle was used because it is the most highly ordered of any vertebrate muscle type (Luther and Squire, 1980;Harford and Squire, 1986).…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

3D Structure of Fish Muscle Myosin Filaments

Eakins

AL-Khayat

Kensler

et al. 2002

Journal of Structural Biology

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

3D Structure of Fish Muscle Myosin Filaments

Eakins

AL-Khayat

Kensler

et al. 2002

Journal of Structural Biology

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“…In this way, the full 43-nm repeat could be reconstructed instead of the structure being averaged onto a 14.3-nm-spaced crown. This same problem was then approached using the rich low-angle X-ray diffraction patterns from bony fish muscle which, with a novel computer program called MOVIE, were modelled with a Class I head arrangement for vertebrate striated muscle filaments to a nominal resolution of about 7 nm, but an effective positional sensitivity of about 1 nm since the known very high resolution myosin head crystal structure was being used (Hudson et al 1997;. This showed slightly different structures on the three crowns of the 43-nm repeat, with two crowns similar but different from the third.…”

Section: Ideas About Head Conformations In Resting Musclementioning

confidence: 99%

Muscle myosin filaments: cores, crowns and couplings

Squire

2009

Biophys Rev

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Myosin filaments in muscle, carrying the ATPase myosin heads that interact with actin filaments to produce force and movement, come in multiple varieties depending on species and functional need, but most are based on a common structural theme. The now successful journeys to solve the ultrastructures of many of these myosin filaments, at least at modest resolution, have not been without their false starts and erroneous sidetracks, but the picture now emerging is of both diversity in the rotational symmetries of different filaments and a degree of commonality in the way the myosin heads are organised in resting muscle. Some of the remaining differences may be associated with how the muscle is regulated. Several proteins in cardiac muscle myosin filaments can carry mutations associated with heart disease, so the elucidation of myosin filament structure to understand the effects of these mutations has a clear and topical clinical relevance.

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“…In the case of oriented polycrystalline materials and high-resolution data, the programs LALS (Arnott & Wonacott, 1966;Arnott et al, 1969;Okada et al, 2003) and FXPLOR Wang & Stubbs, 1993) can be used to refine and test plausible molecular structures. Modelling of helical macromolecular assemblies can be carried out using MOVIE (Hudson et al, 1997;AL-Khayat et al, 2004). A preliminary quick look at the kind of diffraction pattern that helical structures of plausible symmetry and dimensions might produce can be obtained from the HELIX program .…”

Section: Modelling Of Non-crystalline Structuresmentioning

confidence: 99%

The CCP13FibreFixprogram suite: semi-automated analysis of diffraction patterns from non-crystalline materials

et al. 2007

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The extraction of useful information from recorded diffraction patterns from non-crystalline materials is non-trivial and is not a well defined operation. Unlike protein crystallography where one expects to see well behaved diffraction spots in predictable positions defined by standard space groups, the diffraction patterns from non-crystalline materials are very diverse. They can range from uniaxially oriented fibre patterns which are completely sampled as Bragg peaks, but rotationally averaged around the fibre axis, to fibre patterns that are completely unsampled, to either kind of pattern with considerable axial misalignment (disorientation), to liquid-like order and even to mixtures of these various structure types. In the case of protein crystallography, the specimen is generated artificially and only used if the degree of order is sufficient to yield a three-dimensional density map of high enough resolution to be interpreted sensibly. However, with non-crystalline diffraction, many of the specimens of interest are naturally occurring (e.g. cellulose, rubber, collagen, muscle, hair, silk) and to elucidate their structure it is necessary to extract structural information from the materials as they actually are and to whatever resolution is available. Even when synthetic fibres are generated from purified components (e.g. nylon, polyethylene, DNA, polysaccharides, amyloids etc.) and diffraction occurs to high resolution, it is rarely possible to obtain perfect uniaxial alignment. The CCP13 project was established in the 1990s to generate software which will be generally useful for analysis of non-crystalline diffraction patterns. Various individual programs were written which allowed separate steps in the analysis procedure to be carried out. Many of these programs have now been integrated into a single user-friendly package known as FibreFix, which is freely downloadable from http://www.ccp13.ac.uk. Here the main features of FibreFix are outlined and some of its applications are illustrated.

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Myosin head configuration in relaxed fish muscle: resting state myosin heads must swing axially by up to 150 Å or turn upside down to reach rigor

Cited by 63 publications

References 65 publications

3D Structure of Fish Muscle Myosin Filaments

3D Structure of Fish Muscle Myosin Filaments

Muscle myosin filaments: cores, crowns and couplings

The CCP13FibreFixprogram suite: semi-automated analysis of diffraction patterns from non-crystalline materials

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