Crystallization and preliminary X-ray diffraction studies of alpha-amylase from the antarctic psychrophile Alteromonas haloplanctis A23.
International audience 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-ada...
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ftunivlyon1:oai:HAL:hal-00313566v1 2023-05-15T13:44:38+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. Institut de biologie et chimie des protéines Lyon (IBCP) Université Claude Bernard Lyon 1 (UCBL) Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS) 1996 https://hal.science/hal-00313566 en eng HAL CCSD Wiley hal-00313566 https://hal.science/hal-00313566 ISSN: 0961-8368 EISSN: 1469-896X Protein Science https://hal.science/hal-00313566 Protein Science, 1996, 5, pp.2128-2129 [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology info:eu-repo/semantics/article Journal articles 1996 ftunivlyon1 2023-04-07T11:52:55Z International audience 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.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 HAL Lyon 1 (University Claude Bernard Lyon 1) Antarctic The Antarctic |
institution |
Open Polar |
collection |
HAL Lyon 1 (University Claude Bernard Lyon 1) |
op_collection_id |
ftunivlyon1 |
language |
English |
topic |
[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology |
spellingShingle |
[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology 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 |
[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology |
description |
International audience 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.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. |
author2 |
Institut de biologie et chimie des protéines Lyon (IBCP) Université Claude Bernard Lyon 1 (UCBL) Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS) |
format |
Article in Journal/Newspaper |
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 |
HAL CCSD |
publishDate |
1996 |
url |
https://hal.science/hal-00313566 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
ISSN: 0961-8368 EISSN: 1469-896X Protein Science https://hal.science/hal-00313566 Protein Science, 1996, 5, pp.2128-2129 |
op_relation |
hal-00313566 https://hal.science/hal-00313566 |
_version_ |
1766204261907038208 |