Abstract
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 language | English |
|---|---|
| Pages (from-to) | 773-775 |
| Number of pages | 3 |
| Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
| Volume | 65 |
| Issue number | 8 |
| DOIs | |
| Publication status | Published - 19 Aug 2009 |
| Externally published | Yes |
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Keywords
- Camelus dromedarius
- Haemoglobin
- Oxygen affinity
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Structural Biology
- Genetics
- Condensed Matter Physics
Cite this
Purification, crystallization and preliminary crystallographic study of haemoglobin from camel (Camelus dromedarius) : A high oxygen-affinity lowland species. / Moovarkumudalvan, Balasubramanian; Sathya Moorthy, Pon; Neelagandan, K.; Ponnuswamy, M. N.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 65, No. 8, 19.08.2009, p. 773-775.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Purification, crystallization and preliminary crystallographic study of haemoglobin from camel (Camelus dromedarius)
T2 - A high oxygen-affinity lowland species
AU - Moovarkumudalvan, Balasubramanian
AU - Sathya Moorthy, Pon
AU - Neelagandan, K.
AU - Ponnuswamy, M. N.
PY - 2009/8/19
Y1 - 2009/8/19
N2 - 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°.
AB - 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°.
KW - Camelus dromedarius
KW - Haemoglobin
KW - Oxygen affinity
UR - http://www.scopus.com/inward/record.url?scp=68649090989&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=68649090989&partnerID=8YFLogxK
U2 - 10.1107/S1744309109024154
DO - 10.1107/S1744309109024154
M3 - Article
C2 - 19652336
AN - SCOPUS:68649090989
VL - 65
SP - 773
EP - 775
JO - Acta Crystallographica Section F:Structural Biology Communications
JF - Acta Crystallographica Section F:Structural Biology Communications
SN - 1744-3091
IS - 8
ER -