Production of crystals of human aldose reductase with very high resolution diffraction.

Date publication

mars 1999

Auteurs

Membres identifiés du Cancéropôle Est :
Dr MORAS Dino , Dr POTERSZMAN Arnaud , Dr VAN DORSSELAER Alain

Tous les auteurs :
Lamour V, Barth P, Rogniaux H, Poterszman A, Howard E, Mitschler A, Van Dorsselaer A, Podjarny A, Moras D

Lien Pubmed

https://www.ncbi.nlm.nih.gov/pubmed/10089480

Résumé

As the action of human aldose reductase (hAR) is thought to be linked to the pathogenesis of diabetic complications, much effort has been directed towards the analysis of the catalytic mechanism and the development of specific inhibitors. Here, the crystallization of recombinant hAR with its cofactor NADP+ at 277 K in the presence of the precipitating agent PEG 6000 is reported. The crystals diffract to high resolution (1.1 A) and belong to the P21 space group with unit-cell parameters a = 49.97, b = 67.14, c = 48. 02 A, beta = 92.2 degrees with one molecule per asymmetric unit. Seleno-substituted hAR crystals were also produced and diffract to 1. 7 A on a conventional X-ray source.

Référence

Acta Crystallogr D Biol Crystallogr. 1999 Mar;55(Pt 3):721-3.