L773:1097 0134 OR L773:0887 3585
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Purification, crystallization, and preliminary X-ray analysis of Bacillus subtilis ferrochelatase
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- Hansson, Mats (author)
- Lund University,Lunds universitet,Molekylär cellbiologi,Biologiska institutionen,Naturvetenskapliga fakulteten,Molecular Cell Biology,Department of Biology,Faculty of Science,Carlsberg Research Center / Carlsberg Laboratory
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- Al-Karadaghi, Salam (author)
- Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
- (creator_code:org_t)
- Wiley, 1995
- 1995
- English.
- In: Proteins. - : Wiley. - 0887-3585. ; 23:4, s. 607-609
- Journal article (peer-reviewed)
Abstract
Subject headings
Close
- 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.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Keyword
- 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
Publication and Content Type
- art (subject category)
- ref (subject category)
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