title: Crystallization and preliminary X-ray diffraction analysis of maize aldose reductase.
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.
authors.affiliation: Laboratório de Biologia Estrutural, Instituto de Química, Universidade Estadual de Campinas, CP 6154, 13083-970 Campinas-SP, Brazil.
authors.forename: Eduardo
authors.initials: E
authors.lastname: Kiyota
authors.forename: Sylvia Morais
authors.initials: SM
authors.lastname: de Sousa
authors.forename: Marcelo Leite
authors.initials: ML
authors.lastname: Dos Santos
authors.forename: Aline
authors.initials: A
authors.lastname: da Costa Lima
authors.forename: Marcelo
authors.initials: M
authors.lastname: Menossi
authors.forename: José Andrés
authors.initials: JA
authors.lastname: Yunes
authors.forename: Ricardo
authors.initials: R
authors.lastname: Aparicio
mesh_terms: D000449:Aldehyde Reductase / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D003313:Zea mays / Q000201:enzymology*
chemical_list: D000449:Aldehyde Reductase