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  • 1
    Electronic Resource
    Electronic Resource
    Time-Resolved X-Ray Diffraction Studies on Vertebrate Striated Muscle (1983)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Biophysics and Biomolecular Structure 12 (1983), S. 381-417 
    Details
    ISSN: 0084-6589
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.bb.12.060183.002121
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Time-resolved studies on contracting muscle using small-angle X-ray diffraction. I. Design of data collection system (1978)
    Copenhagen : International Union of Crystallography (IUCr)
    Applied crystallography online 11 (1978), S. 449-454 
    Details
    ISSN: 1600-5767
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: Small-angle X-ray diffraction offers a unique method for the study of muscle structure at a molecular level. Structural changes in muscle during contraction can be studied with a 10 ms time resolution with the use of a powerful X-ray generator and electronic detectors. A data-collection system is described which is based on a linear position-sensitive detector capable of synchronizing data from 32 different phases of a muscle contraction cycle and storing it in different subgroups of a multichannel analyzer memory. On completion of an experiment with a muscle the complete data set is transferred via a fast link to a PDP 11/10 computer for processing and storage. A promising approach to the automated analysis of equatorial data is to assume that the pattern is a sum of a polynomial background and Gaussian peaks. A χ2-minimization procedure, which optimizes the parameters used to describe the pattern, gives excellent agreement between experimental data and the proposed model. Finally a detector system is proposed which would allow collection of data at high rates expected from a camera set on a storage ring.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0021889878013734
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Solution small-angle X-ray scattering studies on myosin with a multiwire area detector (1991)
    Copenhagen : International Union of Crystallography (IUCr)
    Applied crystallography online 24 (1991), S. 852-856 
    Details
    ISSN: 1600-5767
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: 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 (6S) form which is capable of forming filaments and generating force and a `folded' (10S) 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 10S form is greater than for the 6S 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 6S form of myosin when both S1 heads are assumed to be close together.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S002188989100047X
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  • 4
    Electronic Resource
    Electronic Resource
    The use of synchrotron radiation in time-resolved X-ray diffraction studies of myosin layer-line reflections during muscle contraction (1980)
    [s.l.] : Nature Publishing Group
    Nature 284 (1980), S. 140-143 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Experiments on striated muscle have been carried out at the EMBL Outstation at DESY, Hamburg, using the electron–positron storage ring DORIS as a high-intensity X-ray source. The low-angle reflections from the myosin cross-bridges could be recorded more than 1,000 times more rapidly than with ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/284140a0
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    Paper (German National Licenses)
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