ISOLATION, CRYSTALLIZATION AND PRELIMINARY DIFFRACTION ANALYSES OF HUMAN PANCREATIC ALPHA-AMYLASE

Human pancreatic α-amylase has been isolated using a glycogen affinity precipitation procedure and crystallized in a form suitable for high resolution three-dimensional X-ray crystallographic analyses. Crystals are of the orthorhombic space group P212121, with unit cell dimensions of a = 53.04 Å, b = 74.80 Å and c = 137.34 Å, and contain only one protein molecule per asymmetric unit. Diffraction data have been collected and found to extend to 1.6 Å resolution. These studies form the basis for elucidating the full atomic structure of human pancreatic α-amylase and thereby providing insight into the catalytic mechanism of this enzyme. © 1993 Academic Press, Inc.