Abstract
Hexameric glucosamine-6-phosphate deaminase from Escherichia coli has been crystallized isomorphously with both phosphate and ammonium sulphate as precipitants, over a wide pH range (6·0 to 9·0). The crystals belong to space ropu R32 and the cell parameters in the hexagonal settings are a = b = 125·9Åandc = 223·2Å. A complete native data set was collected to 2·1Åresolution. Self-rotation function studies suggest that the hexamers sit on the 3-fold axis and have point group symmetry 32, with a non-crystallographic dyad relating two monomers linked by an interchain disulfide bridge. A possible packing for the unit cell is proposed.
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