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The crystal structure of human hemoglobin crosslinked between the Lysβ82 residues has been determined at 2.30 Å resolution. The crosslinking reaction was performed under oxy conditions using bis(3,5-dibromosalicyl) fumarate; the modified hemoglobin has increased oxygen affinity and lacks cooperativity. Since the crystallization occurred under deoxy conditions, the resulting structure displays conformational...
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