Abstract
The three-dimensional structure of the surface layer (S layer) protein of the thermophilic bacterium Clostridium thermohydrosulfuricum has been determined by electron microscopy to a resolution of about 2.5 nm. Two independent reconstructions have been obtained from the top and bottom layers of flattened S-layer sacculi after separation of the lattices in the course of correlation averaging of the projections. In spite of different levels of stain embedding, the two reconstructions agree with each other remarkably well. Six elongated spiral-shaped rods form cup-shaped complexes linked within the p6 lattice via the threefold crystallographic axes.
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