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

• Published in: Acta Crystallographica Section F Structural Biology and Crystallization Communications
• Main Authors: MERLINO, ANTONELLO, MAZZARELLA, LELIO, VERGARA, ALESSANDRO, Vitagliano L, Balsamo A, Nicoletti FP, Howes BD, Giordano D, Coppola D, di Prisco G, Verde C, Smulevich G
• Other Authors: Merlino, Antonello, Vitagliano, L, Balsamo, A, Nicoletti, Fp, Howes, Bd, Giordano, D, Coppola, D, di Prisco, G, Verde, C, Smulevich, G, Mazzarella, Lelio, Vergara, Alessandro
• Format: Article in Journal/Newspaper
• Language: unknown
• Published: 2010
• Subjects: raman; crystallography; hemoglobin; Antarctic; Antarc*
• Online Access: http://hdl.handle.net/11588/373183; https://doi.org/10.1107/S1744309110038698

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 A ̊ 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.