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

Research output: Contribution to journalArticlepeer-review


Bacillus subtilis ferrochelatase (EC, 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
Issue number4
Publication statusPublished - 1995

Bibliographical note


Subject classification (UKÄ)

  • Biochemistry and Molecular Biology


  • 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


Dive into the research topics of 'Purification, crystallization, and preliminary X-ray analysis of Bacillus subtilis ferrochelatase'. Together they form a unique fingerprint.

Cite this