We have renewed our effort to pursue the structural analysis of the tetanus toxin which was grown on the phospholipid along with its natural ganglioside ligand. Our previous analysis suggested the possibility of obtaining high resolution image data beyond 10 ? using flood beam illumination. We plan to vary the crystallization condition to obtain more ordered two-dimensional crystals and to use spot-scan imaging to obtain better images. We feel that this project has a potential to become a core project for the development of high resolution two-dimensional crystal structure analysis in place of the crotoxin complex crystal core project which has been terminated. The significance of this project is partly to solve an unknown protein structure and partly to show the feasibility of determining the high resolution three-dimensional structure of protein crystals grown on phospholipid monolayers.
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