Structural plasticity in the eight-helix fold of a trematode haemoglobin

Mario Milani, Alessandra Pesce, Sylvia Dewilde, Paolo Ascenzi, Luc Moens, Martino Bolognesi

Research output: Contribution to journalArticle


The three-dimensional structure of recombinant haemoglobin from the trematode Paramphistomum epiclitum, displaying the highest oxygen affinity so far observed for (non)vertebrate haemoglobins, has previously been determined at 1.17 Å resolution (orthorhombic space group P212121). In the present communication, the three-dimensional structure of wild-type P. epiclitum haemoglobin is reported at 1.85 Å resolution in a monoclinic crystal form (R factor = 16.1%, Rfree = 22.0%). Comparison of P. epiclitum (recombinant versus wild-type ferric Hb) structures in the two crystal forms shows structural differences in the haem proximal and distal sites which have not been reported for other known haemoglobin structures previously.

Original languageEnglish
Pages (from-to)719-722
Number of pages4
JournalActa Crystallographica Section D: Biological Crystallography
Issue number4
Publication statusPublished - 2002

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics
  • Condensed Matter Physics
  • Structural Biology

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