통합자연과학논문집 (Journal of Integrative Natural Science)

조선대학교 기초과학연구원 (The Basic Science Institute Chosun University)
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Purification, Crystallization, Preliminary X-ray Diffraction and Molecular-Replacement Studies of White-Breasted Water hen (Amaurornis Phoenicurus) Haemoglobin

  • Jagadeesan, G. (Department of Physics, Presidency College) ;
  • Jaimohan, S.M. (Center of Advanced Study in Crystallography and Biophysics, University of Madras) ;
  • Malathy, P. (Biophysics Laboratory, Council of Scientific and Industrial Research- Central Leather Research Institute) ;
  • Aravindhan, S. (Department of Physics, Presidency College)
  • 투고 : 2013.10.31
  • 심사 : 2013.12.20
  • 발행 : 2013.12.30
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초록

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 avian haemoglobins (Hbs). Towards this end, purification, crystallization, preliminary X-ray diffraction and molecular-replacement studies have been carried out on Amaurornis phoenicurus Hb. Crystals were grown by the hanging drop vapor-diffusion method using PEG 2000 and NaCl as precipitants. The crystals belonged to the primitive monoclinic system $P2_1$, with unit-cell parameters $a=65.33{\AA}$, $b=93.14{\AA}$, $c=98.54{\AA}$, ${\beta}=100.48^{\circ}$; a complete data set was collected to a resolution of $2.6{\AA}$. The Matthews coefficient of $2.30{\AA}^3Da^{-1}$ for the crystal indicated the presence of two ${\alpha}_2{\beta}_2$ tetramers in the asymmetric unit.

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