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Crystallization and preliminary X-ray characterization of a PaaX-like protein fromSulfolobus solfataricusP2
- Source :
- Acta Crystallographica Section F Structural Biology and Crystallization Communications. 65:776-778
- Publication Year :
- 2009
- Publisher :
- International Union of Crystallography (IUCr), 2009.
-
Abstract
- PaaX is a global regulator of the phenylacetyl-coenzyme A catabolon that adjusts the expression of different operons to that of the paa-encoded central pathway. In this study, the PaaX-like protein from the hyperthermophilic archaeon Sulfolobus solfataricus P2 was successfully crystallized by the hanging-drop vapour-diffusion method using ammonium sulfate as a precipitant. Diffraction data were obtained to a resolution of 3.0 A using synchrotron radiation at the Photon Factory. The crystal belonged to space group P321, with unit-cell parameters a = 86.4, b = 86.4, c = 105.5 A.
- Subjects :
- Ammonium sulfate
Protein Conformation
Operon
Archaeal Proteins
ved/biology.organism_classification_rank.species
Biophysics
Biology
Crystallography, X-Ray
Polymerase Chain Reaction
Biochemistry
law.invention
Crystal
chemistry.chemical_compound
Protein structure
Structural Biology
law
Genetics
Crystallization
DNA Primers
Base Sequence
ved/biology
Resolution (electron density)
Sulfolobus solfataricus
food and beverages
Space group
Condensed Matter Physics
enzymes and coenzymes (carbohydrates)
Crystallography
chemistry
Crystallization Communications
biological sciences
health occupations
bacteria
Subjects
Details
- ISSN :
- 17443091
- Volume :
- 65
- Database :
- OpenAIRE
- Journal :
- Acta Crystallographica Section F Structural Biology and Crystallization Communications
- Accession number :
- edsair.doi.dedup.....a7263a0d26969349c10badeab84bd7df