Open AccessCrystallization, preliminary X‐ray diffraction studies and Raman microscopy of the major haemoglobin from the sub‐Antarctic fish Eleginops maclovinus in the carbomonoxy form
Author(s) -
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
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110038698
Subject(s) - orthorhombic crystal system , raman spectroscopy , crystallography , crystallization , crystal (programming language) , fish <actinopterygii> , cooperativity , diffraction , chemistry , resolution (logic) , crystal structure , materials science , biology , optics , biochemistry , physics , programming language , organic chemistry , artificial intelligence , fishery , computer science
The blood of the sub‐Antarctic fish Eleginops maclovinus (Em) contains three haemoglobins. The major haemoglobin (Hb1Em) displays the Root effect, a drastic decrease in the oxygen affinity and a loss of cooperativity at acidic pH. The carbomonoxy form of HbEm1 has been crystallized in two different crystal forms, orthorhombic (Ortho) and hexagonal (Hexa), and high‐resolution diffraction data have been collected for both forms (1.45 and 1.49 Å resolution, respectively). The high‐frequency resonance Raman spectra collected from the two crystal forms using excitation at 514 nm were almost indistinguishable. Hb1Em is the first sub‐Antarctic fish Hb 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 haemoglobins.