Abstract
L-Leucine dehydrogenase from Bacillus cereus was examined in the electron microscope. The quaternary structure reveals a molecule that is built up from 8 subunits, identical in mass, arranged in 2 layers which are oriented mainly in a staggered form. In each layer subunits are positioned at the vertices of a square, leaving free a central protein-deficient region of 2.6 nm in diameter. The enzyme measures 11.1 nm in diagonal and 9.0 nm in edge length. Mean subunit diameter is 4.0 nm. The overall shape is a cube, slightly compressed, with 90% edge length in height.
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