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Biophys J, August 2002, p. 1074-1081, Vol. 83, No. 2

Direct X-Ray Observation of a Single Hexagonal Myofilament Lattice in Native Myofibrils of Striated Muscle

Hiroyuki Iwamoto,* Yukihiro Nishikawa,dagger Jun'ichi Wakayama,* and Tetsuro Fujisawadagger

 *Life and Environment Division, SPring-8, Japan Synchrotron Radiation Research Institute, Hyogo 679-5198, Japan; and  dagger Structural Biochemistry Laboratory, RIKEN Harima Institute, SPring-8, Hyogo 679-5148, Japan

A striated muscle fiber consists of thousands of myofibrils with crystalline hexagonal myofilament lattices. Because the lattices are randomly oriented, the fiber gives rise to an equatorial x-ray diffraction pattern, which is essentially a rotary-averaged "powder diffraction," carrying only information about the distance between the lattice planes. We were able to record an x-ray diffraction pattern from a single myofilament lattice, very likely originating from a single myofibril from the flight muscle of a bumblebee, by orienting the incident x-ray microbeam along the myofibrillar axis (end-on diffraction). The pattern consisted of a number of hexagonally symmetrical diffraction spots whose originating lattice planes were readily identified. This also held true for some of the weak higher order reflections. The spot-like appearance of reflections implies that the lattice order is extremely well maintained for a distance of millimeters, covering up to a thousand of ~2.5-µm-long sarcomeres connected in series. The results open the possibility of applying the x-ray microdiffraction technique to study many other micrometer-sized assemblies of functional biomolecules in the cell.

Biophys J, August 2002, p. 1074-1081, Vol. 83, No. 2
© 2002 by the Biophysical Society   0006-3495/02/08/1074/08  $2.00


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[Abstract] [Full Text] [PDF]


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