Expression, purification, crystallization and preliminary X-ray diffraction analysis of thioredoxin Trx1 from Saccharomyces cerevisiae

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Apr 1;64(Pt 4):323-5. doi: 10.1107/S1744309108004612. Epub 2008 Mar 29.

Abstract

Thioredoxins play key roles in the cellular response to oxidative stress. Three isoforms of thioredoxin have been identified in Saccharomyces cerevisiae: two that are cytosolic (Trx1 and Trx2) and one that is mitochondrial (Trx3). In the present work, the cytosolic form Trx1 was cloned, expressed, purified and crystallized. Crystals were obtained by the hanging-drop vapour-diffusion method. A data set was collected from a single crystal to 1.7 A resolution. The crystal belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 32.29, b = 46.59, c = 64.20 A, alpha = beta = gamma = 90 degrees .

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Crystallization
  • Cytosol / chemistry
  • Cytosol / metabolism
  • Gene Expression Regulation, Fungal / physiology*
  • Membrane Proteins / chemistry*
  • Membrane Proteins / genetics
  • Membrane Proteins / isolation & purification
  • Molecular Sequence Data
  • Peroxiredoxins
  • Saccharomyces cerevisiae / chemistry*
  • Saccharomyces cerevisiae / genetics*
  • Saccharomyces cerevisiae / isolation & purification
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / isolation & purification
  • Thioredoxins / biosynthesis
  • Thioredoxins / chemistry*
  • Thioredoxins / genetics
  • Thioredoxins / isolation & purification
  • X-Ray Diffraction*

Substances

  • Membrane Proteins
  • Saccharomyces cerevisiae Proteins
  • TRX1 protein, S cerevisiae
  • Thioredoxins
  • Peroxiredoxins