one publication added to basket [262191] | Crystal structure study of Opsanus tau parvalbumin by multiwavelength anomalous diffraction
Kahn, R.; Fourme, R.; Bosshard, R.; Chiadmi, M.; Risler, J.L.; Dideberg, O.; Wery, J.P. (1985). Crystal structure study of Opsanus tau parvalbumin by multiwavelength anomalous diffraction. FEBS Lett. 179(1): 133-137. dx.doi.org/10.1016/0014-5793(85)80207-6
In: FEBS Letters. ELSEVIER SCIENCE BV: Amsterdam. ISSN 0014-5793; e-ISSN 1873-3468, more
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Keyword |
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Author keywords |
Multiwavelength anomalous diffraction;Protein crystallography;Parvalbumin;Anomalous scattering;Synchrotron radiation;Electronic area detector |
Authors | | Top |
- Kahn, R.
- Fourme, R.
- Bosshard, R.
- Chiadmi, M.
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- Risler, J.L.
- Dideberg, O.
- Wery, J.P.
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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 Å were collected at three wavelengths near the L3 absorption edge of Tb (1.645–1.650 Å), 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. |
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