Isolation, crystallization and preliminary diffraction analyses of human pancreatic alpha-amylase.

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.

journal_name

J Mol Biol

authors

Burk D,Wang Y,Dombroski D,Berghuis AM,Evans SV,Luo Y,Withers SG,Brayer GD

doi

10.1006/jmbi.1993.1221

subject

Has Abstract

pub_date

1993-04-05 00:00:00

pages

1084-5

issue

3

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(83)71221-0

journal_volume

230

pub_type

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