An alpha -amylase originating from a mold Aspergillus oryzae, Taka-amylase A (Mr of 52 kDa, pI of 3.8), has been purified to an electrophoretically single band grade. Crystallization behaviors were investigated using ammonium sulfate and polyethleneglycol 8000 as precipitants. The variations in the morphology of the crystals obtained with changing crystallization parameters are described. Five apparently different crystal forms were obtained, and their morphology and crystallographic data have been determined. Solubility values of four typical forms were measured using a Michelson-type two-beam interferometer. The results of these experiments showed that this protein can be a potentially interesting and useful model for crystal growth study with a gram-amount availability of pure protein sample.