Abstract
X-ray fiber diffraction is a powerful tool used for investigating the molecular structure of muscle and its dynamics during contraction. This technique has been successfully applied not only to skeletal and cardiac muscles of vertebrates but also to insect flight muscle. Generally, insect flight muscle has a highly ordered structure and is often capable of high-frequency oscillations. The X-ray diffraction studies on muscle have been accelerated by the advent of 3rd-generation synchrotron radiation facilities, which can generate brilliant and highly oriented X-ray beams. This review focuses on some of the novel experiments done on insect flight muscle by using synchrotron radiation X-rays. These include diffraction recordings from single myofibrils within a flight muscle fiber by using X-ray microbeams and high-speed diffraction recordings from the flight muscle during the wing-beat of live insects. These experiments have provided information about the molecular structure and dynamic function of flight muscle in unprecedented detail. Future directions of X-ray diffraction studies on muscle are also discussed.
Highlights
Like light microscopy and electron microscopy, X-ray diffraction is one of the techniques used to resolve the fine structure of objects by using the scattering of electromagnetic waves or electron beams
The resolution of protein 3-D structures obtained by single-particle analyses in cryo-electron microscopy used to be worse than 1 nm, but, recently, this has been dramatically changed by the advent of direct detectors, which have nominal pixel sizes equivalent to ~1 Å at the scale of the sample
The real-space image of the object cannot be restored. This is called the phase problem and great efforts have been made to solve the problem in every field of X-ray diffraction studies including protein crystallography
Summary
Like light microscopy and electron microscopy, X-ray diffraction is one of the techniques used to resolve the fine structure of objects by using the scattering of electromagnetic waves or electron beams. The spatial resolution obtained in each technique is defined by the diffraction limit, which is comparable to the wavelength of the beams used Both X-ray beams and the electron beams (used in the electron microscope) have wavelengths comparable to or shorter than the lengths of atomic bonds and, in principle, atomic resolution should be obtained by using both of these techniques. In protein crystallography, such atomic-resolution structures of proteins are routinely obtained. We describe the latest results of research obtained by using this technique and, lastly, we discuss some future direction for X-ray diffraction studies on muscle
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