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Updated: May 17, 2026
Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
Published on: July 5, 2018
Purification, crystallization, preliminary X-ray diffraction and molecular-replacement studies of catfish (Clarias
S M Jaimohan1, M D Naresh, A B Mandal
1Chemical Laboratory, Central Leather Research Institute, Council of Scientific and Industrial Research (CSIR), Adyar, Chennai 600 020, India.
Abstract:
Haemoglobin is an interesting physiologically significant protein composed of specific functional prosthetic haem and globin moieties. In recent decades, there has been substantial interest in attempting to understand the structural basis and functional diversity of fish haemoglobins (Hbs). Towards this end, purification, crystallization, preliminary X-ray diffraction and molecular-replacement studies have been carried out on Clarias magur Hb. Crystals were grown by the hanging-drop vapour-diffusion method using PEG 2000 and NaCl as precipitants. The crystals belonged to the primitive monoclinic system P2, with unit-cell parameters a=98.35, b=56.63, c=112.88 Å, β=100.22°; a complete data set was collected to a resolution of 2.4 Å. The Matthews coefficient of 2.42 Å3 Da(-1) for the crystal indicated the presence of two α2β2 tetramers in the asymmetric unit.
