Expression, purification and X-ray crystallographic analysis of thioredoxin from Streptomyces coelicolor

Petra Stefankova, Jana Maderova, Imrich Barak, Marta Kollarova, Zbyszek Otwinowski

Research output: Contribution to journalArticlepeer-review

4 Scopus citations


Thioredoxins are ubiquitous proteins that serve as reducing agents and general protein disulfide reductases. In turn, they are reduced by electrons obtained from the NADPH-containing thioredoxin reductase. Thioredoxins have been isolated and characterized from a large number of organisms. The Gram-positive bacterium Streptomyces coelicolor contains three thioredoxins that are involved in unknown biological processes. trxA from S. coelicolor was cloned and expressed in Escherichia coli and the protein purified and crystallized using the hanging-drop method of vapour diffusion. The crystal structure of thioredoxin A has been determined at 1.5 Å resolution using a synchrotron-radiation source. The protein reveals a thioredoxin-like fold with a typical CXXC active site. The crystal exhibits the symmetry of space group P21212, with unit-cell parameters a = 43.6, b = 71.8, c = 33.2 Å.

Original languageEnglish (US)
Pages (from-to)164-168
Number of pages5
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue number2
StatePublished - 2005

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics


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