Open AccessPurification, crystallization and preliminary crystallographic studies of haemoglobin from mongoose ( Helogale parvula ) in two different crystal forms induced by pH variation
Author(s) -
Mohamed Abubakkar M.,
Saraboji K.,
Ponnuswamy M. N.
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430911205083x
Subject(s) - orthorhombic crystal system , monoclinic crystal system , chemistry , crystallography , crystallization , oxygen , crystal (programming language) , crystal structure , organic chemistry , computer science , programming language
Haemoglobin (Hb) is a respiratory pigment; it is a tetrameric protein that ferries oxygen from the lungs to tissues and transports carbon dioxide on the return journey. The oxygen affinity of haemoglobin is regulated by the concentration of oxygen surrounding it and several efforts have revealed the shapes of Hb in different states and with different functions. However, study of the molecular basis of Hbs from low‐oxygen‐affinity species is critically needed in order to increase the understanding of the mechanism behind oxygen adaptation. The present study reports the preliminary crystallographic study of low‐oxygen‐affinity haemoglobin from mongoose, a burrowing mammal. Haemoglobin from mongoose was purified by anion‐exchange chromatography, crystallized using the hanging‐drop vapour‐diffusion method and diffraction data sets were collected from monoclinic (2.3 Å resolution) and orthorhombic (2.9 Å resolution) crystal forms obtained by pH variation. The monoclinic and orthorhombic asymmetric units contained half and a whole biological molecule, respectively.