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Crystallization and preliminary X-ray diffraction studies of α-amylase from the antarctic psychrophile Alteromonas haloplanctis A23

✍ Scribed by Nushin Aghajari; Richard Haser; Georges Feller; Charles Gerday

Publisher
Cold Spring Harbor Laboratory Press
Year
1996
Tongue
English
Weight
208 KB
Volume
5
Category
Article
ISSN
0961-8368

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✦ Synopsis

Abstract

A cold‐active α‐amylase was purified from culture supernatants of the antarctic psychrophile Alteromonas haloplanctis A23 grown at 4 °C. In order to contribute to the understanding of the molecular basis of cold adaptations, crystallographic studies of this cold‐adapted enzyme have been initiated because a three‐dimensional structure of a mesophilic counterpart, pig pancreatic α‐amylase, already exists. α‐Amylase from A. haloplanctis, which shares 53% sequence identity with pig pancreatic α‐amylase, has been crystallized and data to 1.85 Å have been collected. The space group is found to be C222~1~ with a = 71.40 Å, b = 138.88 Å, and c = 115.66 Å. Until now, a three‐dimensional structure of a psychrophilic enzyme is lacking.

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