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 language | English |
|---|---|
| Pages (from-to) | 607-609 |
| Journal | Proteins |
| Volume | 23 |
| Issue number | 4 |
| DOIs | |
| Publication status | Published - 1995 |
Bibliographical note
4Subject 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