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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, more
Peer reviewed article  

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Keyword
    Marine
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.
  • Risler, J.L.
  • Dideberg, O.
  • Wery, J.P.

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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