Abstract
α-Amylase has been purified from swine pancreas by adsorption onto glycogen and crystallized from concentrated protein solutions in the presence of Ca 2+. Two morphological forms have been obtained and X-ray analysis has shown them both to be of space group P2 12 12 1 with a = 70 A ̊ , b = 110 A ̊ and c = 117 A ̊ . There are two molecules of total molecular weight 90 000 in the asymmetric unit. The diffraction pattern extends to a resolution of better than 3 Å and appears to be stable to radiation exposure.
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