Crystallization and preliminary X-ray diffraction studies of alpha-amylase from the antarctic psychrophile Alteromonas haloplanctis A23.
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 i...
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Cold Spring Harbor Laboratory Press
1996
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ftpubmed:oai:pubmedcentral.nih.gov:2143274 2023-05-15T13:38:05+02:00 Crystallization and preliminary X-ray diffraction studies of alpha-amylase from the antarctic psychrophile Alteromonas haloplanctis A23. Aghajari, N. Feller, G. Gerday, C. Haser, R. 1996-10 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2143274 http://www.ncbi.nlm.nih.gov/pubmed/8897615 en eng Cold Spring Harbor Laboratory Press http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2143274 http://www.ncbi.nlm.nih.gov/pubmed/8897615 Research Article Text 1996 ftpubmed 2013-09-01T10:27:57Z 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. Text Antarc* Antarctic PubMed Central (PMC) Antarctic The Antarctic |
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Research Article |
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Research Article Aghajari, N. Feller, G. Gerday, C. Haser, R. Crystallization and preliminary X-ray diffraction studies of alpha-amylase from the antarctic psychrophile Alteromonas haloplanctis A23. |
topic_facet |
Research Article |
description |
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. |
format |
Text |
author |
Aghajari, N. Feller, G. Gerday, C. Haser, R. |
author_facet |
Aghajari, N. Feller, G. Gerday, C. Haser, R. |
author_sort |
Aghajari, N. |
title |
Crystallization and preliminary X-ray diffraction studies of alpha-amylase from the antarctic psychrophile Alteromonas haloplanctis A23. |
title_short |
Crystallization and preliminary X-ray diffraction studies of alpha-amylase from the antarctic psychrophile Alteromonas haloplanctis A23. |
title_full |
Crystallization and preliminary X-ray diffraction studies of alpha-amylase from the antarctic psychrophile Alteromonas haloplanctis A23. |
title_fullStr |
Crystallization and preliminary X-ray diffraction studies of alpha-amylase from the antarctic psychrophile Alteromonas haloplanctis A23. |
title_full_unstemmed |
Crystallization and preliminary X-ray diffraction studies of alpha-amylase from the antarctic psychrophile Alteromonas haloplanctis A23. |
title_sort |
crystallization and preliminary x-ray diffraction studies of alpha-amylase from the antarctic psychrophile alteromonas haloplanctis a23. |
publisher |
Cold Spring Harbor Laboratory Press |
publishDate |
1996 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2143274 http://www.ncbi.nlm.nih.gov/pubmed/8897615 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2143274 http://www.ncbi.nlm.nih.gov/pubmed/8897615 |
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1766101427834322944 |