Crystallization, preliminary X-ray diffraction studies and Raman microscopy of the major haemoglobin from the sub-Antarctic fish Eleginops maclovinus in the carbomonoxy form

The major haemoglobin of the sub-Antarctic fish E. maclovinus is the first sub-Antarctic fish haemoglobin to be crystallized and its structural characterization will shed light on the molecular mechanisms of cold adaptation and the role of the Root effect in fish.

Bibliographic Details
Published in:Acta Crystallographica Section F Structural Biology and Crystallization Communications
Main Authors: Merlino, Antonello, Vitagliano, Luigi, Balsamo, Anna, Nicoletti, Francesco P., Howes, Barry D., Giordano, Daniela, Coppola, Daniela, di Prisco, Guido, Verde, Cinzia, Smulevich, Giulietta, Mazzarella, Lelio, Vergara, Alessandro
Format: Text
Language:English
Published: International Union of Crystallography 2010
Subjects:
Crystallization Communications
Antarctic
Antarc*
Online Access:http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3001669
http://www.ncbi.nlm.nih.gov/pubmed/21045316
https://doi.org/10.1107/S1744309110038698
Description
Summary:The major haemoglobin of the sub-Antarctic fish E. maclovinus is the first sub-Antarctic fish haemoglobin to be crystallized and its structural characterization will shed light on the molecular mechanisms of cold adaptation and the role of the Root effect in fish.

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