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Updated: Jun 23, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Structure of amyloid fibrils of hen egg white lysozyme studied by microbeam X-ray diffraction
Naoto Yagi1, Noboru Ohta, Tatsuhito Matsuo
1Japan Synchrotron Radiation Research Institute, SPring-8, Sayo, 1-1-1 Kouto, Hyogo, Japan. yagi@spring8.or.jp
Abstract:
Structure of spherical aggregates formed by hen egg white lysozyme (HEWL) was studied with microbeam X-ray diffraction. Aggregates with a diameter of 50-100 microm were formed after incubation of HEWL at pH 1.6 and 60 degrees C up to 60 days. The scattering from the aggregate in solution showed a marked symmetry demonstrating it as a spherulite. A reflection at 1/0.46 nm(-1) along the fiber axis showed the presence of beta-sheets along the fiber. There were strong equatorial reflections at 1/2.4 and 1/1.2 nm(-1). The similarities to other amyloid fibers suggest that molecules are planar in the direction perpendicular to the fiber axis and beta-strands are making hydrogen bonds to neighboring molecules.
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