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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Sep 1;68(Pt 9):1098-101. doi: 10.1107/S1744309112030527. Epub 2012 Aug 31.

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%.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Crystallization
  • Crystallography, X-Ray
  • Molecular Sequence Data
  • Oxidoreductases / chemistry*
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Vibrio vulnificus / enzymology*

Substances

  • Oxidoreductases