Purification, crystallization and preliminary X-ray diffraction analysis of theStaphylococcus epidermidisextracellular serine protease Esp
| Autor: | Krishnan Vengadesan, Sthanam V.L. Narayana, Tadayuki Iwase, Yoshimitsu Mizunoe, Shinya Sugumoto, Kevin Macon |
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| Rok vydání: | 2012 |
| Předmět: |
Protein Conformation
Biophysics Crystallography X-Ray medicine.disease_cause Biochemistry law.invention fluids and secretions Protein structure Bacterial Proteins Structural Biology law Staphylococcus epidermidis Thermolysin Genetics Extracellular medicine Cloning Molecular Crystallization Serine protease Chromatography biology Serine Endopeptidases Biofilm biochemical phenomena metabolism and nutrition Condensed Matter Physics biology.organism_classification Crystallization Communications Staphylococcus aureus biology.protein |
| Zdroj: | Acta Crystallographica Section F Structural Biology and Crystallization Communications. 69:49-52 |
| ISSN: | 1744-3091 |
| Popis: | Esp, an extracellular serine protease from Staphylococcus epidermidis, has been shown to inhibit S. aureus biofilm formation and nasal colonization. The full-length 27 kDa pro-Esp was purified and digested with thermolysin to obtain mature Esp. The mature Esp containing 216 residues crystallized in space group P2(1), with unit-cell parameters a = 39.5, b = 61.2, c = 42.5 Å, β = 98.2° and one molecule in the asymmetric unit, with an estimated solvent content of 42%. A diffraction data set has been collected to 1.8 Å resolution on a rotating-anode home-source facility. |
| Databáze: | OpenAIRE |
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