Crystallization, preliminary X-ray diffraction analysis and Patterson search of oxyhaemoglobin I from the wolf (Chrysocyon brachiurus)

Oxyhaemoglobin I isolated from the Brazilian wolf Chrysocyon brachiurus has been crystallized and X‐ray diffraction data has been collected to 2.06 Å resolution using a synchrotron‐radiation source. Crystals were determined to belong to the space group P212121 and preliminary structural analysis rev...

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Bibliographic Details
Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 1999-09, Vol.55 (9), p.1618-1619
Main Authors: Smarra, A. L. S., Fadel, V., Dellamano, M., Olivieri, J. R., De Azevedo Jr, W. F., Bonilla-Rodriguez, G. O.
Format: Article
Language:English
Subjects:
allosteric control
Animals
Crystallization
oxyhaemoglobin I
Oxyhemoglobins - chemistry
Rotation
Wolves - blood
X-Ray Diffraction
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Summary:Oxyhaemoglobin I isolated from the Brazilian wolf Chrysocyon brachiurus has been crystallized and X‐ray diffraction data has been collected to 2.06 Å resolution using a synchrotron‐radiation source. Crystals were determined to belong to the space group P212121 and preliminary structural analysis revealed the presence of one tetramer in the asymmetric unit. The structure was determined using standard molecular‐replacement techniques and is currently being refined using maximum‐likelihood protocols. This is the first haemoglobin isolated from a member of the Canidae family to be crystallized and it will provide further insights in the comparative biochemistry of vertebrate haemoglobins.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444999009725