Structural studies on the loggerhead sea turtle (Caretta caretta) myoglobin

R. Petruzzelli, G. Aureli, E. Casale, M. Nardini, M. Rizzi, P. Ascenzi, M. Coletta, G. De Sanctis, A. Desideri, A. Galteri, M. Bolognesi

Research output: Contribution to journalArticlepeer-review


The primary structure of myoglobin from the loggerhead sea turtle (Caretta caretta) has been determined; the protein consists of 153 amino acid residues. The ferric loggerhead sea turtle myoglobin has been crystallized in a form suitable for X-ray structural investigations. The crystals were grown at pH 8.0, in 0.05 M tris/HCl buffer, using 3.2 M ammonium sulfate as precipitating agent, at 4°C, and belong to the orthorhombic space group P212121, with unit cell constants a = 37.2 Å, b = 61.1 Å, c = 75.2 Å (one molecule, 17,000 M(r), in the asymmetric unit). A molecular replacement solution was found for the loggerhead sea turtle myoglobin crystals using sperm whale myoglobin structure as search model. The R-factor value, after molecular replacement, is 0.387, for the data in the 15-3.3 Å resolution range. The results here reported are the basis for the first X-ray crystallographic investigation on a reptile myoglobin, and indicate a strong overall structural similarity between the loggerhead sea turtle and mammalian (i.e. sperm whale) myoglobins.

Original languageEnglish
Pages (from-to)19-24
Number of pages6
JournalBiochemistry and Molecular Biology International
Issue number1
Publication statusPublished - 1993

ASJC Scopus subject areas

  • Biochemistry
  • Genetics
  • Molecular Biology


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