Isolation, Crystallization and Preliminary Diffraction Analyses of Human Pancreatic α-Amylase

• Published in: Journal of molecular biology Vol. 230; no. 3; pp. 1084 - 1085
• Main Authors: Burk, David, Wang, Yili, Dombroski, Dennise, Berghuis, Albert M., Evans, Stephen V., Luo, Yaoguang, Withers, Stephen G., Brayer, Gary D.
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier Ltd 05.04.1993; Elsevier
• Subjects: alpha-amylase; alpha-Amylases - chemistry; alpha-Amylases - isolation & purification; amylase; Biological and medical sciences; crystal structures; Crystalline structure; Crystallization; Fundamental and applied biological sciences. Psychology; Humans; Molecular biophysics; molecular conformation; pancreas; Pancreas - enzymology; pancreatic; starch; Structure in molecular biology; X-Ray Diffraction; crystallization; pancreatic; starch; amylase; Human; Unit cell; Enzyme; Affinity chromatography; Crystallization; Isolation; α-Amylase; Pancreas; X ray diffraction
• ISSN: 0022-2836; 1089-8638
• DOI: 10.1006/jmbi.1993.1221

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 P2 12 12 1, 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 elucidating the full atomic structure of human pancreative α-amylase and thereby providing insight into the catalytic mechaism of this enzyme.