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A survey of 129 protein crystal structures with more than one molecule per asymmetric unit shows that local (non-crystallographic) symmetry axes are not randomly oriented. When compared to the crystal cell edges, face diagonals, body diagonal and reciprocal cell edges, 65% of the local symmetry axes are found to be parallel to one of the reference directions to within 15°; another 18% are orthogonal to within 3°; only 17% are in general orientations. In monoclinic, trigonal and hexagonal crystals, a majority of the local symmetry axes are orthogonal to the unique axis, while preferred orientations are parallel to the cell edges in orthorhombic crystals.
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