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

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 cofacto...

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Bibliographic Details
Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 1999-03, Vol.55 (3), p.721-723
Main Authors: Lamour, V., Barth, P., Rogniaux, H., Poterszman, A., Howard, E., Mitschler, A., Van Dorsselaer, A., Podjarny, A., Moras, D.
Format: Article
Language:English
Subjects:
Aldehyde Reductase - chemistry
Aldehyde Reductase - isolation & purification
aldose reductase
Biochemistry, Molecular Biology
Crystallization
Crystallography, X-Ray
Humans
Life Sciences
Mass Spectrometry
oxidoreductases
Recombinant Proteins - chemistry
Recombinant Proteins - isolation & purification
Structural Biology
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Summary: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 Å) and belong to the P21 space group with unit‐cell parameters a = 49.97, b = 67.14, c = 48.02 Å, β = 92.2° with one molecule per asymmetric unit. Seleno‐substituted hAR crystals were also produced and diffract to 1.7 Å on a conventional X‐ray source.
ISSN:1399-0047
0907-4449
2059-7983
1399-0047
2059-7983
DOI:10.1107/S0907444998013365