Literature DB >> 22949204

Crystallization and preliminary X-ray crystallographic analysis of the putative NADP(H)-dependent oxidoreductase YncB from Vibrio vulnificus.

Min-Kyu Kim1, Young Jun An, Chang-Sook Jeong, Sun-Shin Cha.   

Abstract

The yncB gene product from Vibrio vulnificus, which belongs to the medium-chain dehydrogenase/reductase (MDR) superfamily, was crystallized using the microbatch crystallization method at 295 K. Diffraction data sets were collected using synchrotron radiation. Crystals of selenomethionine-substituted YncB protein belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 90.52, b = 91.56, c = 104.79 Å. Assuming the presence of two molecules in the asymmetric unit, the solvent content was estimated to be about 57%. Crystals of the YncB-NADP(H) complex belonged to space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 90.14, c = 105.61 Å. Assuming the presence of one molecule in the asymmetric unit, the solvent content was estimated to be about 56.42%.

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Year:  2012        PMID: 22949204      PMCID: PMC3433207          DOI: 10.1107/S1744309112030527

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


  20 in total

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Authors:  K J Edwards; J D Barton; J Rossjohn; J M Thorn; G L Taylor; D L Ollis
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Journal:  Eur J Biochem       Date:  1994-11-15

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  1 in total

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  1 in total

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