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

Research output: Contribution to journalArticle

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.

Details

Authors
Organisations
External organisations
  • Carlsberg Research Center / Carlsberg Laboratory
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • 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
Original languageEnglish
Pages (from-to)607-609
JournalProteins
Volume23
Issue number4
Publication statusPublished - 1995
Publication categoryResearch
Peer-reviewedYes

Bibliographic note

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