Abstract
The structure of the protein crystals formed by Bacillus thuringiensis Berliner, determined from electron micrographs of shadowed carbon replicas of dry crystals, can be described by a tetramolecular face-centered-cubic unit cell 123 A on an edge. The protein molecules appear to be spherical, with a diameter D = 87 A. The bipyramidal shape of these crystals results from their being bounded by eight similar (221) faces on which the rows of molecules are separated by 3 D. Membrane fragments made up of hexagonal arrays of spheres or ellipsoids whose average center-to-center separation is 68 A were common in the preparations examined and were believed to be a component of the cell walls.
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