Crystallization and preliminary X-ray diffraction studies of a-amylase from the antarctic psychrophile Alteromonas haloplanctis A23
peer reviewed 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 enzy...
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1996
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Online Access: | https://orbi.uliege.be/handle/2268/17106 https://orbi.uliege.be/bitstream/2268/17106/1/ProtSci_1996_AHA.pdf https://doi.org/10.1002/pro.5560051021 |
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ftorbi:oai:orbi.ulg.ac.be:2268/17106 2024-04-21T07:51:31+00:00 Crystallization and preliminary X-ray diffraction studies of a-amylase from the antarctic psychrophile Alteromonas haloplanctis A23 Aghajari, N. Feller, Georges Gerday, Charles Haser, R. 1996 https://orbi.uliege.be/handle/2268/17106 https://orbi.uliege.be/bitstream/2268/17106/1/ProtSci_1996_AHA.pdf https://doi.org/10.1002/pro.5560051021 en eng Wiley-Blackwell urn:issn:0961-8368 urn:issn:1469-896X https://orbi.uliege.be/handle/2268/17106 info:hdl:2268/17106 https://orbi.uliege.be/bitstream/2268/17106/1/ProtSci_1996_AHA.pdf doi:10.1002/pro.5560051021 scopus-id:2-s2.0-0029962635 info:pmid:8897615 open access http://purl.org/coar/access_right/c_abf2 info:eu-repo/semantics/openAccess Protein Science: A Publication of the Protein Society, 5 (10), 2128-2129 (1996) Life sciences Biochemistry biophysics & molecular biology Sciences du vivant Biochimie biophysique & biologie moléculaire journal article http://purl.org/coar/resource_type/c_6501 info:eu-repo/semantics/article peer reviewed 1996 ftorbi https://doi.org/10.1002/pro.5560051021 2024-03-27T14:52:24Z peer reviewed 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. Article in Journal/Newspaper Antarc* Antarctic University of Liège: ORBi (Open Repository and Bibliography) Protein Science 5 10 2128 2129 |
institution |
Open Polar |
collection |
University of Liège: ORBi (Open Repository and Bibliography) |
op_collection_id |
ftorbi |
language |
English |
topic |
Life sciences Biochemistry biophysics & molecular biology Sciences du vivant Biochimie biophysique & biologie moléculaire |
spellingShingle |
Life sciences Biochemistry biophysics & molecular biology Sciences du vivant Biochimie biophysique & biologie moléculaire Aghajari, N. Feller, Georges Gerday, Charles Haser, R. Crystallization and preliminary X-ray diffraction studies of a-amylase from the antarctic psychrophile Alteromonas haloplanctis A23 |
topic_facet |
Life sciences Biochemistry biophysics & molecular biology Sciences du vivant Biochimie biophysique & biologie moléculaire |
description |
peer reviewed 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 |
Article in Journal/Newspaper |
author |
Aghajari, N. Feller, Georges Gerday, Charles Haser, R. |
author_facet |
Aghajari, N. Feller, Georges Gerday, Charles Haser, R. |
author_sort |
Aghajari, N. |
title |
Crystallization and preliminary X-ray diffraction studies of a-amylase from the antarctic psychrophile Alteromonas haloplanctis A23 |
title_short |
Crystallization and preliminary X-ray diffraction studies of a-amylase from the antarctic psychrophile Alteromonas haloplanctis A23 |
title_full |
Crystallization and preliminary X-ray diffraction studies of a-amylase from the antarctic psychrophile Alteromonas haloplanctis A23 |
title_fullStr |
Crystallization and preliminary X-ray diffraction studies of a-amylase from the antarctic psychrophile Alteromonas haloplanctis A23 |
title_full_unstemmed |
Crystallization and preliminary X-ray diffraction studies of a-amylase from the antarctic psychrophile Alteromonas haloplanctis A23 |
title_sort |
crystallization and preliminary x-ray diffraction studies of a-amylase from the antarctic psychrophile alteromonas haloplanctis a23 |
publisher |
Wiley-Blackwell |
publishDate |
1996 |
url |
https://orbi.uliege.be/handle/2268/17106 https://orbi.uliege.be/bitstream/2268/17106/1/ProtSci_1996_AHA.pdf https://doi.org/10.1002/pro.5560051021 |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
Protein Science: A Publication of the Protein Society, 5 (10), 2128-2129 (1996) |
op_relation |
urn:issn:0961-8368 urn:issn:1469-896X https://orbi.uliege.be/handle/2268/17106 info:hdl:2268/17106 https://orbi.uliege.be/bitstream/2268/17106/1/ProtSci_1996_AHA.pdf doi:10.1002/pro.5560051021 scopus-id:2-s2.0-0029962635 info:pmid:8897615 |
op_rights |
open access http://purl.org/coar/access_right/c_abf2 info:eu-repo/semantics/openAccess |
op_doi |
https://doi.org/10.1002/pro.5560051021 |
container_title |
Protein Science |
container_volume |
5 |
container_issue |
10 |
container_start_page |
2128 |
op_container_end_page |
2129 |
_version_ |
1796934866382618624 |