Literature DB >> 15299738

X-ray structure of a new crystal form of pike 4.10 beta parvalbumin.

J P Declercq1, B Tinant, J Parello.   

Abstract

A new crystal form of pike (pI 4.10) parvalbumin has been crystallized in presence of EDTA at pH 8.0. The crystals are orthorhombic, space group P2(1)2(1)2(1), with a = 51.84, b = 49.95, c = 34.96 A. Diffractometer data were collected to 1.75 A. The structure was solved by molecular replacement and refined to R = 0.168 for 7774 observed reflections [I>/= 2sigma(I)] in the range 8.0-1.75 A. In spite of the presence of EDTA, calcium ions are present in both primary binding sites. As compared to the previously reported structures, the main differences concern the conformation of the N-terminal residues and the packing in the unit cell.

Entities:  

Year:  1996        PMID: 15299738     DOI: 10.1107/S0907444995010006

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  2 in total

1.  Crystal structure of the EF-hand parvalbumin at atomic resolution (0.91 A) and at low temperature (100 K). Evidence for conformational multistates within the hydrophobic core.

Authors:  J P Declercq; C Evrard; V Lamzin; J Parello
Journal:  Protein Sci       Date:  1999-10       Impact factor: 6.725

2.  Hydration-coupled dynamics in proteins studied by neutron scattering and NMR: the case of the typical EF-hand calcium-binding parvalbumin.

Authors:  J M Zanotti; M C Bellissent-Funel; J Parello
Journal:  Biophys J       Date:  1999-05       Impact factor: 4.033

  2 in total

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