X-ray crystallographic studies of metalloproteins.

Abstract : Many proteins require metals for their physiological function. In combination with spectroscopic characterizations, X-ray crystallography is a very powerful method to correlate the function of protein-bound metal sites with their structure. Due to their special X-ray scattering properties, specific metals may be located in metalloprotein structures and eventually used for phasing the diffracted X-rays by the method of Multi-wavelength Anomalous Dispersion (MAD). How this is done is the principle subject of this chapter. Attention is also given to the crystallographic characterization of different oxidation states of redox active metals and to the complication of structural changes that may be induced by X-ray irradiation of protein crystals.
Type de document :
Article dans une revue
Methods in Molecular Biology -Clifton then Totowa-, Humana Press (Springer Imprint), 2014, 1122, pp.189-206
Liste complète des métadonnées

http://hal.univ-grenoble-alpes.fr/hal-01119802
Contributeur : Frank Thomas <>
Soumis le : mardi 24 février 2015 - 09:59:11
Dernière modification le : jeudi 11 janvier 2018 - 06:15:24

Identifiants

  • HAL Id : hal-01119802, version 1
  • PUBMED : 24639261

Collections

UGA | CEA | IBS | IBS-MET | DSV

Citation

Anne Volbeda. X-ray crystallographic studies of metalloproteins.. Methods in Molecular Biology -Clifton then Totowa-, Humana Press (Springer Imprint), 2014, 1122, pp.189-206. 〈hal-01119802〉

Partager

Métriques

Consultations de la notice

65