Bacterial expression of Scapharca dimeric hemoglobin: A simple model system for investigating protein cooperativity

Candace M. Summerford, Animesh Pardanani, Andrew H. Betts, Anthony R. Poteete, Gianni Colotti, William E. Royer

Research output: Contribution to journalArticle

24 Scopus citations


Recombinant Scapharca homodimeric hemoglobin has been expressed at high levels from a synthetic gene in Escherichia coli. Addition of the heme precursor δ-aminolevulinic acid to the expression culture results in a considerable increase in the yield of soluble hemoglobin. The recombinant hemoglobin exhibits cooperative oxygen binding properties indistinguishable from native protein. Crystals of the recombinant protein, like those of native hemoglobin, diffract to high resolution which will allow functional studies of site-directed mutants to be correlated with detailed structural analyses.

Original languageEnglish (US)
Pages (from-to)593-599
Number of pages7
JournalProtein Engineering, Design and Selection
Issue number6
StatePublished - Jun 1 1995


ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Biochemistry
  • Molecular Biology

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