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 diffract to better than 1 Å resolution at the Cornell High Energy Synchrotron Source (CHESS) and are highly stable in the synchrotron radiation. The space group is P212121 and cell dimensions are a = 34.9 Å, b = 61.0 Å, c = 72.5 Å.
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Autor | Pangborn, Walter Erman, Mary Li, Naiyin Burkhart, Brian M. Pletnev, Vladimir Z. Duax, William L. Gutiérrez Ilabaca, Rodrigo Antonio Peirano, Alessandra Eyzaguirre, Jaime Thiel, Daniel J. Ghosh, Debashis |
Título | Characterization of crystals of Penicillium purpurogenum acetyl xylan esterase from high-resolution X-ray diffraction |
Revista | Proteins: Structure, Function, and Bioinformatics |
Volumen | 24 |
Número de publicación | 4 |
Página inicio | 523 |
Página final | 524 |
Fecha de publicación | 1996 |
Resumen | 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 diffract to better than 1 Å resolution at the Cornell High Energy Synchrotron Source (CHESS) and are highly stable in the synchrotron radiation. The space group is P212121 and cell dimensions are a = 34.9 Å, b = 61.0 Å, c = 72.5 Å. |
Derechos | acceso restringido |
DOI | 10.1002/(SICI)1097-0134(199604)24:4<523 |
Enlace | |
Palabra clave | Esterase Crystallography Crystallization Synchrotron radiation |
Temática | Medicina y salud |
Tipo de documento | artículo |