Purification, crystallization, and preliminary X-ray analysis of Bacillus subtilis ferrochelatase
(1995) In Proteins 23(4). p.607-609- 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.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/8001513
- author
- Hansson, Mats LU and Al-Karadaghi, Salam LU
- organization
- publishing date
- 1995
- type
- Contribution to journal
- publication status
- published
- subject
- 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
- in
- Proteins
- volume
- 23
- issue
- 4
- pages
- 607 - 609
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- scopus:0029586760
- pmid:8749860
- ISSN
- 0887-3585
- DOI
- 10.1002/prot.340230419
- language
- English
- LU publication?
- yes
- additional info
- 4
- id
- 7d6ea0ec-357e-46a5-93d4-394349558e18 (old id 8001513)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/8749860
- date added to LUP
- 2016-04-01 16:35:45
- date last changed
- 2024-01-11 11:01:58
@article{7d6ea0ec-357e-46a5-93d4-394349558e18, 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.}}, author = {{Hansson, Mats and Al-Karadaghi, Salam}}, issn = {{0887-3585}}, 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}}, language = {{eng}}, number = {{4}}, pages = {{607--609}}, publisher = {{John Wiley & Sons Inc.}}, series = {{Proteins}}, title = {{Purification, crystallization, and preliminary X-ray analysis of Bacillus subtilis ferrochelatase}}, url = {{http://dx.doi.org/10.1002/prot.340230419}}, doi = {{10.1002/prot.340230419}}, volume = {{23}}, year = {{1995}}, }