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

被引：44

作者：

Lamour, V

Barth, P

Rogniaux, H

Poterszman, A

Howard, E

Mitschler, A

Van Dorsselaer, A

Podjarny, A

Motas, D

机构：

[1] IGBMC, UPR Biol Struct, F-67404 Illkirch Graffenstaden, France

[2] Univ Louis Pasteur Strasbourg 1, Lab Chim Organ Biol, CNRS, URA 31, Strasbourg, France

[3] Univ Louis Pasteur Strasbourg 1, Lab Spectrometrie Masse Bioorgan, CNRS, URA 31, Strasbourg, France

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1999年 / 55卷

关键词：

D O I：

10.1107/S0907444998013365

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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 Angstrom) and belong to the P2(1) space group with unit-cell parameters a = 49.97, b = 67.14, c = 48.02 Angstrom, beta = 92.2 degrees with one molecule per asymmetric unit. Seleno-substituted hAR crystals were also produced and diffract to 1.7 Angstrom on a conventional X-ray source.

引用

页码：721 / 723

页数：3

共 8 条

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[3]

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