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Crystal structure study of Opsanus tau parvalbumin by multiwavelength anomalous diffraction
Author(s) -
Kahn R.,
Fourme R.,
Bosshard R.,
Chiadmi M.,
Risler J.L.,
Dideberg O.,
Wery J.P.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80207-6
Subject(s) - parvalbumin , crystallography , biophysics , chemistry , diffraction , physics , biology , optics , neuroscience
The crystal structure of a small calcium‐binding protein, the parvalbumin III f 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 L 3 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.