Crystallization and preliminary crystallographic analysis of p40phox, a regulatory subunit of NADPH oxidase
| Autor: | Hideki Sumimoto, Satoru Yuzawa, Kazuya Honbou, Yuko Fujioka, Fuyuhiko Inagaki, Nobuo Suzuki |
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| Rok vydání: | 2006 |
| Předmět: |
Protein subunit
Biophysics macromolecular substances Polyethylene glycol Crystallography X-Ray medicine.disease_cause Biochemistry law.invention Crystal chemistry.chemical_compound Structural Biology law Genetics medicine Humans Cloning Molecular Crystallization Escherichia coli NADPH oxidase biology Chemistry Superoxide NADPH Oxidases Space group Condensed Matter Physics enzymes and coenzymes (carbohydrates) Protein Subunits Crystallography Crystallization Communications biological sciences health occupations biology.protein bacteria |
| Zdroj: | Acta Crystallographica Section F Structural Biology and Crystallization Communications. 62:1018-1020 |
| ISSN: | 1744-3091 |
| Popis: | p40(phox) is a cytosolic component of the phagocyte NADPH oxidase, which is responsible for production of the superoxide that kills invasive microorganisms. Full-length p40(phox) was expressed in Escherichia coli, purified and crystallized by the sitting-drop vapour-diffusion method at 293 K using polyethylene glycol 20,000 as a precipitant. Diffraction data were collected to 3.0 A resolution at 100 K using synchrotron radiation. The crystal belongs to space group C222(1), with unit-cell parameters a = 146.27, b = 189.81, c = 79.88 A. This crystal was estimated to contain two or three protein molecules per asymmetric unit from the acceptable range of volume-to-weight ratio values. |
| Databáze: | OpenAIRE |
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