Isolation, crystallization and preliminary diffraction analyses of human pancreatic alpha-amylase.
Human pancreatic alpha-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(1)2(1)2(1), with unit cell dimensions of a = 53.04 A, b = 74.80 A and c = 137.34 A, and contain only one protein molecule per asymmetric unit. Diffraction data have been collected and found to extend to 1.6 A resolution. These studies form the basis for elucidating the full atomic structure of human pancreatic alpha-amylase and thereby providing insight into the catalytic mechanism of this enzyme.
Burk
D
D
Department of Biochemistry, University of British Columbia, Vancouver, Canada.
Wang
Y
Y
Dombroski
D
D
Berghuis
A M
AM
Evans
S V
SV
Luo
Y
Y
Withers
S G
SG
Brayer
G D
GD
D003460:Crystallization; D006801:Humans; D010179:Pancreas / Q000201:enzymology*; D014961:X-Ray Diffraction; D000516:alpha-Amylases / Q000737:chemistry* / Q000302:isolation & purification
D000516:alpha-Amylases