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Crystal structure study of Opsanus tau parvalbumin by multiwavelength anomalous diffraction.
- Source :
-
FEBS letters [FEBS Lett] 1985 Jan 01; Vol. 179 (1), pp. 133-7. - Publication Year :
- 1985
-
Abstract
- 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.
Details
- Language :
- English
- ISSN :
- 0014-5793
- Volume :
- 179
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- FEBS letters
- Publication Type :
- Academic Journal
- Accession number :
- 3965297
- Full Text :
- https://doi.org/10.1016/0014-5793(85)80207-6