Characterization of crystals ofPenicillium purpurogenum acetyl xylan esterase from high-resolution X-ray diffraction
| Autor: | N. Li, Jaime Eyzaguirre, Rodrigo A. Gutiérrez, William L. Duax, Walter Pangborn, B. M. Burkhart, Daniel J. Thiel, Vladimir Z. Pletnev, Alessandra Peirano, Mary Erman, Debashis Ghosh |
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| Rok vydání: | 1996 |
| Předmět: |
animal structures
biology Chemistry Resolution (electron density) Penicillium purpurogenum food and beverages macromolecular substances biology.organism_classification Biochemistry Xylan Esterase Synchrotron law.invention Crystallography Structural Biology law X-ray crystallography Side chain Crystallization Molecular Biology |
| Zdroj: | Proteins: Structure, Function, and Genetics. 24:523-524 |
| ISSN: | 1097-0134 0887-3585 |
| DOI: | 10.1002/(sici)1097-0134(199604)24:4<523::aid-prot13>3.0.co;2-n |
| Popis: | Acetyl xylan esterase from Penicillium purpurogenum, a single-chain 23 kDa member of a newly characterized family of esterases that cleaves side chain ester linkages in xylan, has been crystallized. The crystals dif- fract to better than 1 A resolution at the Cornell High Energy Synchrotron Source (CHESS) and are highly stable in the synchrotron radiation. The space group is P2,2,2' and cell dimensions |
| Databáze: | OpenAIRE |
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