Crystal structure study of Opsanus tau parvalbumin by multiwavelength anomalous diffraction.
The crystal structure of a small calcium-binding protein, the parvalbumin IIIf from Opsanus tau in which Tb was substituted for Ca, has been analysed by multiwavelength anomalous diffraction. Data at a resolution of 2.3 A were collected at three wavelengths near the L3 absorption edge of Tb (1.645-1.650 A), using the synchrotron radiation emitted by a storage ring and a multiwire proportional counter. The phases of the reflections were determined from this single derivative, without native data. Prior to any refinement, the resulting electron density map shows a good agreement with the model of the homologous carp parvalbumin in regions of identical amino-acid sequence.
D000818:Animals; D002347:Carps; D005399:Fishes; D008958:Models, Molecular; D009124:Muscle Proteins; D010320:Parvalbumins; D011487:Protein Conformation; D013045:Species Specificity; D014961:X-Ray Diffraction
D009124:Muscle Proteins; D010320:Parvalbumins