Human neuroglobin: Crystals and preliminary X-ray diffraction analysis

Alessandra Pesce, Marco Nardini, Sylvia Dewilde, Paolo Ascenzi, Thorsten Burmester, Thomas Hankeln, Luc Moens, Martino Bolognesi

Research output: Contribution to journalArticlepeer-review


Neuroglobin, a recently discovered member of the haemoglobin superfamily, is primarily expressed in the brain of humans and other vertebrates, where it has been proposed to enhance O2 supply in response to hypoxia or ischaemia, protecting the neuron from hypoxic injury. Neuroglobin is the first example of a vertebrate haemoglobin in which a hexacoordinate haem geometry has been detected. A triple mutant (replacing three Cys residues) of human neuroglobin (151 amino acids) has been expressed in Escherichia coli, purified and crystallized in two crystal forms, the best of which diffracts to 1.95 Å resolution using synchrotron radiation. The crystals belong to space group P21, with unit-cell parameters a = 39.6, b = 94.9, c = 67.5 Å, β = 94.4°, and contain 2-4 protein molecules per asymmetric unit.

Original languageEnglish
Pages (from-to)1848-1850
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Issue number10 I
Publication statusPublished - Oct 1 2002

ASJC Scopus subject areas

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


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