Electron diffraction and high-resolution imaging on highly-crystalline β-chitin microfibril.

The ultrastructure of β-chitin microfibrils from a centric diatom, Thalassiosira, and a tubeworm, Lamellibrachia, was studied using electron diffraction and high-resolution electron microscopy. Electron microdiffraction diagrams corresponding to each projection of the β-chitin crystals were obtained, and all the data support the structure model of anhydrous β-chitin crystals proposed by X-ray diffraction experiments. From high-resolution electron microscopy on ultrathin sections, the cross-sectional shapes of the microfibrils from Thalassiosira and Lamellibrachia were observed as a rectangular and parallelogram, respectively. The lattice fringes corresponding to the (010) plane of anhydrous β-chitin crystals were clearly observed in both cross-sections. Based on these observations, we have constructed a molecular packing model for β-chitin microfibrils.