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.
Hansson
M
M
Department of Microbiology, Lund University, Sweden.
Al-Karadaghi
S
S
D001412:Bacillus subtilis / Q000201:enzymology* / Q000235:genetics; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D012321:DNA-Directed RNA Polymerases; D004926:Escherichia coli; D005294:Ferrochelatase / Q000737:chemistry* / Q000302:isolation & purification; D005798:Genes, Bacterial; D010957:Plasmids; D011092:Polyethylene Glycols; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D014764:Viral Proteins
D011994:Recombinant Proteins; D014764:Viral Proteins; D011092:Polyethylene Glycols; C062210:bacteriophage T7 RNA polymerase; D012321:DNA-Directed RNA Polymerases; D005294:Ferrochelatase