Purification, crystallization and preliminary crystallographic study of haemoglobin from camel (Camelus dromedarius): A high oxygen-affinity lowland species

Balasubramanian Moovarkumudalvan, Pon Sathya Moorthy, K. Neelagandan, M. N. Ponnuswamy

Research output: Contribution to journalArticle

3 Citations (Scopus)


Haemoglobin is a prototypical allosteric protein that is mainly involved in the transportation of oxygen from the lungs to tissues and of carbon dioxide back to the lungs in an intrinsically coordinated manner to maintain the viability of cells. Haemoglobin from Camelus dromedarius provides an interesting case study of adaptation to life in deserts at extremely high temperatures. An ambition to unravel the integrated structural and functional aspects of the casual survival of this animal at high temperatures led us to specifically work on this problem. The present work reports the preliminary crystallographic study of camel haemo-globin. Camel blood was collected and the haemoglobin was purified by anion-exchange chromatography and crystallized using the hanging-drop vapour-diffusion method under buffered high salt concentration using PEG 3350 as a precipitant. Intensity data were collected using a MAR 345 dtb image-plate detector system. Camel haemo-globin crystallized in the monoclinic space group P21, with one whole biological molecule (α 2Β 2) in the asymmetric unit and unit-cell parameters a = 52.759, b = 116.782, c = 52.807 Å, Β = 120.07°.

Original languageEnglish
Pages (from-to)773-775
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue number8
Publication statusPublished - 19 Aug 2009
Externally publishedYes



  • Camelus dromedarius
  • Haemoglobin
  • Oxygen affinity

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Structural Biology
  • Genetics
  • Condensed Matter Physics

Cite this