Production of crystals of human aldose reductase with very high resolutiondiffraction

As the action of human aldose reductase (hAR) is thought to be linked to th e pathogenesis of diabetic complications, much effort has been directed tow ards the analysis of the catalytic mechanism and the development of specifi c inhibitors. Here, the crystallization of recombinant hAR with its cofacto r NADP(+) at 277 K in the presence of the precipitating agent PEG 6000 is r eported. 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 uni t. Seleno-substituted hAR crystals were also produced and diffract to 1.7 A ngstrom on a conventional X-ray source.