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Updated: Jan 21, 2026

Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases
Published on: November 21, 2010
The crystal structure of haemoglobin from Atlantic cod
Ronny Helland1, Eva Katrin Bjørkeng1, Ulli Rothweiler1
1NorStruct, Department of Chemistry, Faculty of Science and Technology, UiT - The Arctic University of Norway, NO-9037 Tromsø, Norway.
The crystal structure of Atlantic cod haemoglobin was determined. This research reveals potential polymorphism in its tetrameric assembly, offering insights into fish haemoglobin structure.
Area of Science:
- Biochemistry
- Structural Biology
- Marine Biology
Background:
- Haemoglobin (Hb) is crucial for oxygen transport in vertebrates.
- Understanding fish Hb structure provides insights into adaptation to aquatic environments.
- Atlantic cod (Gadus morhua) is an ecologically and economically important species.
Purpose of the Study:
- To determine the high-resolution crystal structure of Atlantic cod haemoglobin.
- To investigate the quaternary structure and potential variations in cod Hb assembly.
Main Methods:
- X-ray crystallography was employed to solve the crystal structure.
- The structure was refined to a resolution of 2.54 Å.
- Analysis of the crystallographic asymmetric unit was performed.
Main Results:
- The crystal structure of Atlantic cod haemoglobin was successfully resolved.
- The asymmetric unit contains two distinct tetrameric haemoglobin molecules.
- Structural analysis suggests the possibility of polymorphism in the tetrameric assembly of cod Hb.
Conclusions:
- The determined crystal structure provides a detailed molecular model of Atlantic cod haemoglobin.
- Evidence for tetrameric assembly polymorphism in cod Hb was observed.
- This finding contributes to the understanding of structural diversity in fish haemoglobins.
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