Chaperone-assisted expression of authentic bovine adrenodoxin reductase in Escherichia coli

Clemens Vonrhein, Ulrich Schmidt, Gabriele A. Ziegler, Susann Schweiger, Israel Hanukoglu, Georg E. Schulz

Research output: Contribution to journalArticlepeer-review

23 Scopus citations


Adrenodoxin reductase is an essential component of the mitochondrial monooxygenase systems that are involved in the synthesis of steroid hormones and related compounds. After removing by mutagenesis a secondary ribosome binding site and an mRNA loop formed between the gene and the vector, large amounts of the enzyme could be produced in Escherichia coli by coexpression with the HSP60-chaperone system. The purified protein was homogeneous enough for reproducible crystallization. The crystals diffracted X-rays isotropically beyond 1.7 A resolution permitting a structure analysis. Copyright (C) 1999 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)167-169
Number of pages3
JournalFEBS Letters
Issue number2
StatePublished - 29 Jan 1999


  • Adrenodoxin reductase
  • Chaperone coexpression
  • Crystallization
  • Secondary ribosome binding site
  • mRNA loop


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