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.
|Number of pages||6|
|Journal||Biochemistry and Molecular Biology International|
|Publication status||Published - 1993|
ASJC Scopus subject areas
- Molecular Biology