The crystal structure of a high oxygen affinity species of haemoglobin (bar-headed goose haemoglobin in the oxy form).

doi:10.1006/jmbi.1996.0040

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Article

The crystal structure of a high oxygen affinity species of haemoglobin (bar-headed goose haemoglobin in the oxy form).

Journal of molecular biology - 26 Jan 1996

Zhang J, Hua Z, Tame J R, Lu G, Zhang R, Gu X

Abstract excerpt

We have determined the crystal structure of bar-headed goose haemoglobin in the oxy form to a resolution of 2.0 A. The R-factor of the model is 19.8%. The structure is similar to human HbA, but contacts between the subunits show slightly altered packing of the tetramer. Bar-headed goose blood sho...

Topics

2,3-Diphosphoglycerate
Animals
Crystallization
Crystallography, X-Ray
Diphosphoglyceric Acids
Geese
Heme
Hemoglobins
Humans
Inositol Phosphates
Mutation
Oxygen
Oxyhemoglobins
Protein Conformation

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