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Crystallization and diffraction analysis of thioredoxin reductase from Streptomyces coelicolor
- Source :
- Acta crystallographica. Section F, Structural biology and crystallization communications. 67(Pt 8)
- Publication Year :
- 2011
-
Abstract
- Thioredoxin reductases are homodimeric flavoenzymes that catalyze the transfer of electrons from NADPH to oxidized thioredoxin substrate. Bacterial thioredoxin reductases represent a promising target for the development of new antibiotics. Recombinant thioredoxin reductase TrxB from Streptomyces coelicolor was crystallized using the hanging-drop vapour-diffusion method. X-ray diffraction data were collected from cryocooled crystals to 2.4 Å resolution using a synchrotron-radiation source. The crystals belonged to the primitive monoclinic space group P2(1), with unit-cell parameters a = 82.9, b = 60.6, c = 135.4 Å, α = γ = 90.0, β = 96.5°.
- Subjects :
- Thioredoxin-Disulfide Reductase
Thioredoxin reductase
Biophysics
Streptomyces coelicolor
Crystallography, X-Ray
Biochemistry
law.invention
Structural Biology
law
Genetics
Crystallization
biology
fungi
Substrate (chemistry)
Ferredoxin-thioredoxin reductase
Condensed Matter Physics
biology.organism_classification
Crystallography
enzymes and coenzymes (carbohydrates)
Crystallization Communications
biological sciences
Recombinant DNA
health occupations
bacteria
Thioredoxin
Subjects
Details
- ISSN :
- 17443091
- Volume :
- 67
- Issue :
- Pt 8
- Database :
- OpenAIRE
- Journal :
- Acta crystallographica. Section F, Structural biology and crystallization communications
- Accession number :
- edsair.doi.dedup.....33473d6113463fbf112f76e5efff3f04