Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/197539
Type: Artigo de periódico
Title: Crystallization And Preliminary X-ray Diffraction Analysis Of Maize Aldose Reductase.
Author: Kiyota, Eduardo
de Sousa, Sylvia Morais
Dos Santos, Marcelo Leite
da Costa Lima, Aline
Menossi, Marcelo
Yunes, José Andrés
Aparicio, Ricardo
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.
Subject: Aldehyde Reductase
Crystallization
Crystallography, X-ray
Zea Mays
Rights: aberto
Identifier DOI: 10.1107/S1744309107052670
Address: http://www.ncbi.nlm.nih.gov/pubmed/18007059
Date Issue: 2007
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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