Purification, crystallization, and preliminary X-ray analysis of Bacillus subtilis ferrochelatase

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Abstract

Bacillus subtilis ferrochelatase (EC 4.99.1.1), the final enzyme in protoheme IX biosynthesis, was produced with an inducible T7 RNA polymerase expression system in Escherichia coli and purified from the soluble cell fraction. It was crystallized from polyethylene glycol solution using the microseeding technique. The crystals diffract to a minimum Bragg spacing of 2.1 A. The space group is P4(2) with unit cell dimensions a = b = 50.2 A, c = 120.1 A.
Original languageEnglish
Pages (from-to)607-609
JournalProteins
Volume23
Issue number4
DOIs
Publication statusPublished - 1995

Bibliographical note

4

Subject classification (UKÄ)

  • Biochemistry and Molecular Biology

Keywords

  • Genes
  • Ferrochelatase/*chemistry/isolation & purification
  • Escherichia coli
  • X-Ray
  • DNA-Directed RNA Polymerases
  • Crystallography
  • Crystallization
  • Molecular
  • Bacillus subtilis/*enzymology/genetics
  • Cloning
  • Bacterial
  • Plasmids
  • Polyethylene Glycols
  • *Protein Conformation
  • Recombinant Proteins/chemistry/isolation & purification
  • Viral Proteins

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