title: Expression, purification, crystallization and preliminary X-ray analysis of maleylacetate reductase from Burkholderia sp. strain SJ98.
creator: Chauhan, Archana
creator: Islam, Zeyaul
creator: Jain, R K
creator: Karthikeyan, Subramanian
subject: QD Chemistry
description: Maleylacetate reductase (EC 1.3.1.32) is an important enzyme that is involved in the degradation pathway of aromatic compounds and catalyzes the reduction of maleylacetate to 3-oxoadipate. The gene pnpD encoding maleylacetate reductase in Burkholderia sp. strain SJ98 was cloned, expressed in Escherichia coli and purified by affinity chromatography. The enzyme was crystallized in both native and SeMet-derivative forms by the sitting-drop vapour-diffusion method using PEG 3350 as a precipitant at 293 K. The crystals belonged to space group P2(1)2(1)2, with unit-cell parameters a = 72.91, b = 85.94, c = 53.07 A. X-ray diffraction data for the native and SeMet-derivative crystal were collected to 2.7 and 2.9 A resolution, respectively.
publisher: Wiley
date: 2009-12-01
type: Article
type: PeerReviewed
format: application/pdf
identifier: http://crdd.osdd.net/open/538/1/Karthi-acta10.pdf
relation: http://journals.iucr.org/f/issues/2009/12/00/us5002/us5002.pdf
identifier:   Chauhan, Archana and Islam, Zeyaul and Jain, R K and Karthikeyan, Subramanian  (2009) Expression, purification, crystallization and preliminary X-ray analysis of maleylacetate reductase from Burkholderia sp. strain SJ98.  Acta crystallographica. Section F, Structural biology and crystallization communications, 65 (Pt 12).  pp. 1313-6.  ISSN 1744-3091     
relation: http://crdd.osdd.net/open/538/