Expression, purification, crystallization, and preliminary X-ray diffraction analysis of the homodimeric bacterial hemoglobin from Vitreoscilla stercoraria

Cataldo Tarricone, Sabina Calogero, Alessandro Galizzi, Alessandro Coda, Paolo Ascenzi, Martino Bolognesi

Research output: Contribution to journalArticlepeer-review

Abstract

The recombinant homodimeric hemoglobin from the strictly aerobe gram- negative bacterium Vitreoscilla stercoraria has been expressed in Escherichia coli, purified to homogeneity, and crystallized by vapor diffusion techniques, using ammonium sulfate as precipitant. The crystals belong to the monoclinic space group P21 and diffract to HIGH resolution. The unit cell parameters are a = 62.9, b = 42.5, c = 63.2 Å, β = 106.6°; the asymmetric unit contains the homodimeric hemoglobin, with a volume solvent content of 42%.

Original languageEnglish
Pages (from-to)154-156
Number of pages3
JournalProteins: Structure, Function and Genetics
Volume27
Issue number1
DOIs
Publication statusPublished - 1997

Keywords

  • crystal growth
  • dimeric bacterial hemoglobin
  • Vitreoscilla stercoraria
  • x- ray diffraction

ASJC Scopus subject areas

  • Genetics
  • Structural Biology
  • Biochemistry

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