Article (Scientific journals)
Crystallization and preliminary X-ray diffraction studies of a-amylase from the antarctic psychrophile Alteromonas haloplanctis A23
Aghajari, N.; Feller, Georges; Gerday, Charles et al.
1996In Protein Science: A Publication of the Protein Society, 5 (10), p. 2128-2129
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Abstract :
[en] A cold-active alpha-amylase was purified from culture supernatants of the antarctic psychrophile Alteromonas haloplanctis A23 grown at 4 degrees 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 alpha-amylase, already exists. alpha-Amylase from A. haloplanctis, which shares 53% sequence identity with pig pancreatic alpha-amylase, has been crystallized and data to 1.85 A have been collected. The space group is found to be C222(1) with a = 71.40 A, b = 138.88 A, and c = 115.66 A. Until now, a three-dimensional structure of a psychrophilic enzyme is lacking.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Aghajari, N.
Feller, Georges  ;  Université de Liège - ULiège > Département des sciences de la vie > Labo de biochimie
Gerday, Charles ;  Université de Liège - ULiège > Services généraux (Faculté des sciences) > Relations académiques et scientifiques (Sciences)
Haser, R.
Language :
English
Title :
Crystallization and preliminary X-ray diffraction studies of a-amylase from the antarctic psychrophile Alteromonas haloplanctis A23
Publication date :
1996
Journal title :
Protein Science: A Publication of the Protein Society
ISSN :
0961-8368
eISSN :
1469-896X
Publisher :
Wiley-Blackwell, United States - New York
Volume :
5
Issue :
10
Pages :
2128-2129
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 27 January 2010

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