Crystallization and preliminary X-ray diffraction analysis of beta-cinnamomin, an elicitin secreted by the phytopathogenic fungus Phytophthora cinnamomin
| Autor: | Mariaarménia Carrondo, M. L. Rodrigues, Alfredo Cravador, Margarida Archer, Ralph Biemans, M. Aurélio |
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| Jazyk: | angličtina |
| Rok vydání: | 2000 |
| Předmět: |
Models
Molecular Phytophthora Hypersensitive response Ammonium sulfate Protein Conformation Stereochemistry Recombinant Fusion Proteins Resistance Triclinic crystal system Biology Crystallography X-Ray Pichia law.invention Microbiology Fungal Proteins chemistry.chemical_compound Necrosis Structural Biology law Protein Elicitors PEG ratio Tobacco Crystallization Algal Proteins Proteins Elicitin General Medicine biology.organism_classification Ribosome Inactivating Proteins Type 2 chemistry X-ray crystallography Capsicein Member |
| Zdroj: | Repositório Científico de Acesso Aberto de Portugal Repositório Científico de Acesso Aberto de Portugal (RCAAP) instacron:RCAAP |
| Popis: | Cinnamomin (CIN) belongs to a family of 10 kDa proteins designated as elicitins. Some of these proteins induce a hypersensitive response in diverse plant species, leading to resistance against fungal and bacterial plant pathogens. CIN was crystallized by the vapour-diffusion method using either ammonium sulfate or polyethyleneglycol (PEG) as precipitants in solutions buffered at around pH 7. These crystals are isomorphous and belong to the triclinic space group, with unit-cell parameters a = 31.69, b = 36.99, c = 44.09 Angstrom, alpha = 76.86, beta = 84.41, gamma = 80.26 degrees. A frozen crystal diffracted X-rays beyond 1.45 Angstrom resolution on a synchrotron-radiation source. info:eu-repo/semantics/publishedVersion |
| Databáze: | OpenAIRE |
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