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

• 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.

Ämnesord

NATURVETENSKAP  -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)

NATURAL SCIENCES  -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)

Nyckelord

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

Publikations- och innehållstyp

art (ämneskategori)

ref (ämneskategori)