Crystallization and preliminary crystallographic studies of glucosamine-6-phosphate deaminase from Escherichia coli K12. |
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| Authors: | E Horjales M M Altamirano M L Calcagno Z Dauter K Wilson R C Garratt G Oliva |
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| Institution: | Instituto de Física e Química de S?o Carlos, Universidade de S?o Paulo, Brazil. |
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| 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 group R32 and the cell parameters in the hexagonal setting are a = b = 125.9 A and c = 223.2 A. A complete native data set was collected to 2.1 A resolution. 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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