Work

Crystal structure study of Opsanus tau parvalbumin by multiwavelength anomalous diffraction

Year: 1985

Type: article

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.

Source: FEBS Letters

DOI: 10.1016/0014-5793(85)80207-6

Authors: R. Kahn, R. Fourme, R. Bosshard, M. Chiadmi, J.L. Risler, O. Dideberg, J.P. Wery

Institutions: Université Paris-Sud, Centre National de la Recherche Scientifique, Université Paris-Est Créteil, Centre de Génétique Moléculaire, University of Liège

Language: English

Topic: Enzyme Structure and Function

Subfield: Materials Chemistry

Field: Materials Science

Domain: Physical Sciences

Open Access status: bronze

Funder: CERN

OpenAlex ID: W2010543715

FWCI: 3.777

Cites: 21

Cited by: 62

Related to: 10