Crystallization and crystallographic analysis of human NUDT16

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jul 1;64(Pt 7):639-40. doi: 10.1107/S1744309108016928. Epub 2008 Jun 11.

Abstract

Human NUDT16, a decapping enzyme belonging to the Nudix superfamily, plays a pivotal role in U8 snoRNA stability. Recombinant NUDT16 expressed in Escherichia coli was crystallized using the hanging-drop vapour-diffusion method. The crystals, which diffracted to 2.10 A resolution, belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 44.47, b = 79.32, c = 97.20 A. The Matthews coefficient and the solvent content were calculated to be 1.92 A(3) Da(-1) and 35.84%, respectively, for two molecules per asymmetric unit.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Humans
  • Pyrophosphatases / biosynthesis
  • Pyrophosphatases / chemistry*
  • Pyrophosphatases / genetics
  • RNA Caps / biosynthesis
  • RNA Caps / chemistry
  • RNA Caps / genetics
  • RNA, Small Nuclear / chemistry
  • RNA, Small Nuclear / genetics
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics

Substances

  • RNA Caps
  • RNA, Small Nuclear
  • Recombinant Proteins
  • Nudt16 protein, human
  • Pyrophosphatases