Abstract
Publisher Summary Many pyridoxal phosphate (pyridoxal-P) dependent enzymes have been crystallized, but few of the crystals have been studied either by X-ray crystallography or by other physical techniques. Recently, three groups have initiated crystallographic studies on aspartate aminotransferases. The cytosolic enzyme from chicken hearts and from pig hearts has been prepared in orthorhombic forms, while the mitochondrial isoenzyme of chicken heart has been crystallized in a triclinic form. Many pyridoxal-P enzymes form very small and relatively insoluble crystals. However, if the solubility of these enzymes is increased by changing the pH or ionic composition of the buffer, it may be possible to use the polyethyleneglycol method to obtain larger crystals. This chapter describes the preparation of crystals of the cytosolic isoenzyme of aspartate aminotransferase from pig heart and crystals of enzyme-substrate or enzyme-inhibitor complexes. Crystals of enzyme containing analogs of pyridoxal-P can be prepared by reconstituting the apoenzyme and then treating it as above for the native enzyme.
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