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Crystallization and preliminary X-ray diffraction analysis of the azoreductase PpAzoR fromPseudomonas putidaMET94
- Source :
- Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67:121-123
- Publication Year :
- 2010
- Publisher :
- International Union of Crystallography (IUCr), 2010.
-
Abstract
- PpAzoR, an FMN-dependent NADPH azoreductase from Pseudomonas putida MET94, has been crystallized using the sitting-drop vapour-diffusion technique. The crystals diffracted to 1.6 A resolution using synchrotron radiation and belonged to the orthorhombic space group F222, with unit-cell parameters a = 72.1, b = 95.5, c = 146.1 A. Data sets were collected from the native protein to 2.2 A resolution using in-house equipment and to 1.6 A resolution using synchrotron radiation and the three-dimensional structure was determined by the molecular-replacement method.
- Subjects :
- inorganic chemicals
Diffraction
animal structures
Materials science
Protein Conformation
Molecular Sequence Data
Biophysics
Synchrotron radiation
Crystallography, X-Ray
Biochemistry
law.invention
Bacterial Proteins
Structural Biology
law
Genetics
Native protein
NADH, NADPH Oxidoreductases
Crystallization
biology
Pseudomonas putida
Resolution (electron density)
Nitroreductases
Condensed Matter Physics
biology.organism_classification
Crystallography
Crystallization Communications
biological sciences
X-ray crystallography
bacteria
Orthorhombic crystal system
Subjects
Details
- ISSN :
- 17443091
- Volume :
- 67
- Database :
- OpenAIRE
- Journal :
- Acta Crystallographica Section F Structural Biology and Crystallization Communications
- Accession number :
- edsair.doi.dedup.....1553ced8dcfddf6d28cde45eb495792f
- Full Text :
- https://doi.org/10.1107/s1744309110048220