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

@article{Aghajari1996CrystallizationAP,
  title={Crystallization and preliminary X-ray diffraction studies of alpha-amylase from the antarctic psychrophile Alteromonas haloplanctis A23.},
  author={Nushin Aghajari and Georges Feller and Charles Gerday and Richard Haser},
  journal={Protein science : a publication of the Protein Society},
  year={1996},
  volume={5 10},
  pages={2128-9}
}
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… CONTINUE READING

Connections & Topics

Mentioned Connections BETA
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 .
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 .
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 .
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 .
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 .
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 .
All Topics