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Purification, Crystallization, Preliminary X-ray Diffraction and Molecular-Replacement Studies of White-Breasted Water hen (Amaurornis Phoenicurus) Haemoglobin

원문정보

초록

영어

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 P21, with unit-cell parameters a = 65.33 Å, b = 93.14 Å, c = 98.54 Å, β = 100.48o; a complete data set was collected to a resolution of 2.6 Å. The Matthews coefficient of 2.30 Å3 Da-1 for the crystal indicated the presence of two α2β2 tetramers in the asymmetric unit.

목차

Abstract
 1. Introduction
 2. Experimental Section
  2.1. Isolation and Purification
  2.2. Crystallization and X-ray Data Collection
 3. Results and Discussion
 4. Conclusions
 References

저자정보

  • G. Jagadeesan Department of Physics, Presidency College, Chennai 600 005, India
  • S. M. Jaimohan Center of Advanced Study in Crystallography and Biophysics, University of Madras, Chennai 600 025, India
  • P. Malathy Biophysics Laboratory, Council of Scientific and Industrial Research- Central Leather Research Institute, Adyar, Chennai 600 020, India
  • S. Aravindhan Department of Physics, Presidency College, Chennai 600 005, India

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