The crystal structure of haemoglobin from Atlantic cod

The crystal structure of haemoglobin from Atlantic cod has been solved to 2.54 A˚ resolution. The structure consists of two tetramers in the crystallographic asymmetric unit. The structure of haemoglobin obtained from one individual cod suggests polymorphism in the tetrameric assembly. publishedVers...

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Published in:Acta Crystallographica Section F Structural Biology Communications
Main Authors: Helland, Ronny, Bjørkeng, Eva Katrin, Rothweiler, Ulli, Sydnes, Magne Olav, Pampanin, Daniela Maria
Format: Article in Journal/Newspaper
Language:English
Published: 2019
Subjects:
Online Access:https://hdl.handle.net/11250/2648945
https://doi.org/10.1107/S2053230X1900904X
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spelling ftnorce:oai:norceresearch.brage.unit.no:11250/2648945 2023-05-15T15:26:21+02:00 The crystal structure of haemoglobin from Atlantic cod Helland, Ronny Bjørkeng, Eva Katrin Rothweiler, Ulli Sydnes, Magne Olav Pampanin, Daniela Maria 2019 application/pdf https://hdl.handle.net/11250/2648945 https://doi.org/10.1107/S2053230X1900904X eng eng Acta Crystallographica. Section F : Structural Biology and Crystallization Communications. 2019, F75 (8), 537-542. urn:issn:1744-3091 https://hdl.handle.net/11250/2648945 https://doi.org/10.1107/S2053230X1900904X cristin:1714439 CC BY 4.0 https://creativecommons.org/licenses/by/4.0/ CC-BY Acta Crystallographica. Section F : Structural Biology and Crystallization Communications F75 8 537-542 Peer reviewed Journal article 2019 ftnorce https://doi.org/10.1107/S2053230X1900904X 2022-10-13T05:50:31Z The crystal structure of haemoglobin from Atlantic cod has been solved to 2.54 A˚ resolution. The structure consists of two tetramers in the crystallographic asymmetric unit. The structure of haemoglobin obtained from one individual cod suggests polymorphism in the tetrameric assembly. publishedVersion Article in Journal/Newspaper atlantic cod NORCE vitenarkiv (Norwegian Research Centre) Acta Crystallographica Section F Structural Biology Communications 75 8 537 542
institution Open Polar
collection NORCE vitenarkiv (Norwegian Research Centre)
op_collection_id ftnorce
language English
description The crystal structure of haemoglobin from Atlantic cod has been solved to 2.54 A˚ resolution. The structure consists of two tetramers in the crystallographic asymmetric unit. The structure of haemoglobin obtained from one individual cod suggests polymorphism in the tetrameric assembly. publishedVersion
format Article in Journal/Newspaper
author Helland, Ronny
Bjørkeng, Eva Katrin
Rothweiler, Ulli
Sydnes, Magne Olav
Pampanin, Daniela Maria
spellingShingle Helland, Ronny
Bjørkeng, Eva Katrin
Rothweiler, Ulli
Sydnes, Magne Olav
Pampanin, Daniela Maria
The crystal structure of haemoglobin from Atlantic cod
author_facet Helland, Ronny
Bjørkeng, Eva Katrin
Rothweiler, Ulli
Sydnes, Magne Olav
Pampanin, Daniela Maria
author_sort Helland, Ronny
title The crystal structure of haemoglobin from Atlantic cod
title_short The crystal structure of haemoglobin from Atlantic cod
title_full The crystal structure of haemoglobin from Atlantic cod
title_fullStr The crystal structure of haemoglobin from Atlantic cod
title_full_unstemmed The crystal structure of haemoglobin from Atlantic cod
title_sort crystal structure of haemoglobin from atlantic cod
publishDate 2019
url https://hdl.handle.net/11250/2648945
https://doi.org/10.1107/S2053230X1900904X
genre atlantic cod
genre_facet atlantic cod
op_source Acta Crystallographica. Section F : Structural Biology and Crystallization Communications
F75
8
537-542
op_relation Acta Crystallographica. Section F : Structural Biology and Crystallization Communications. 2019, F75 (8), 537-542.
urn:issn:1744-3091
https://hdl.handle.net/11250/2648945
https://doi.org/10.1107/S2053230X1900904X
cristin:1714439
op_rights CC BY 4.0
https://creativecommons.org/licenses/by/4.0/
op_rightsnorm CC-BY
op_doi https://doi.org/10.1107/S2053230X1900904X
container_title Acta Crystallographica Section F Structural Biology Communications
container_volume 75
container_issue 8
container_start_page 537
op_container_end_page 542
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