Crystallization and preliminary X-ray diffraction analysis of maize aldose reductase

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Nov 1;63(Pt 11):990-2. doi: 10.1107/S1744309107052670. Epub 2007 Oct 26.

Abstract

Maize aldose reductase (AR) is a member of the aldo-keto reductase superfamily. In contrast to human AR, maize AR seems to prefer the conversion of sorbitol into glucose. The apoenzyme was crystallized in space group P2(1)2(1)2(1), with unit-cell parameters a = 47.2, b = 54.5, c = 100.6 A and one molecule in the asymmetric unit. Synchrotron X-ray diffraction data were collected and a final resolution limit of 2.0 A was obtained after data reduction. Phasing was carried out by an automated molecular-replacement procedure and structural refinement is currently in progress. The refined structure is expected to shed light on the functional/enzymatic mechanism and the unusual activities of maize AR.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aldehyde Reductase / chemistry*
  • Crystallization
  • Crystallography, X-Ray
  • Zea mays / enzymology*

Substances

  • Aldehyde Reductase