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Crystallization (Commentary)
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2.4.1.14
hanging-drop vapor diffusion technique at 25°C. Crystal structure of SPS and its complexes with the substrate D-fructose 6-phosphate and the product D-sucrose-6'-phosphate. SPS has two distinct Rossmann-fold domains with a large substrate binding cleft at the interdomain interface. Structures of two complexes show that both the substrate D-fructose 6-phosphate and the product D-fructose 6'-phosphate bind to the A-domain of SPS. Halothermothrix orenii may represent a valid model for the catalytic domain of plant SPSs and thus may provide useful insight into the reaction mechanism of the plant enzyme
689470
2.4.1.14
spsA protein crystallized in the monocyclic space group C2, with unit-cell parameters a = 154.2, b = 47.9, c = 103.16°, using hanging-drop vapour-diffusion method. Crystals diffract X-rays to a resolution limit of 3.01 A
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