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Crystallization and preliminary X‐ray diffraction studies of α‐amylase from the antarctic psychrophile Alteromonas haloplanctis A23
Author(s) -
Aghajari Nushin,
Haser Richard,
Feller Georges,
Gerday Charles
Publication year - 1996
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560051021
Subject(s) - psychrophile , alteromonas , mesophile , amylase , cold shock domain , extremophile , enzyme , biology , thermophile , microbiology and biotechnology , biochemistry , crystallography , chemistry , bacteria , genetics , rna , gene
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.