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- W2007702282 abstract "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." @default.
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- W2007702282 date "1993-04-01" @default.
- W2007702282 modified "2023-09-27" @default.
- W2007702282 title "Isolation, Crystallization and Preliminary Diffraction Analyses of Human Pancreatic α-Amylase" @default.
- W2007702282 doi "https://doi.org/10.1006/jmbi.1993.1221" @default.
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