Characterization of crystals of Penicillium purpurogenum acetyl xylan esterase from high-resolution X-ray diffraction
Abstract
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 Angstrom resolution at the Cornell High Energy Synchrotron Source (CHESS) and are highly stable in the synchrotron radiation, The space group is P2(1)2(1)2(1) and cell dimensions are a = 34.9 Angstrom, b = 61.0 Angstrom, c = 72.5 Angstrom. (C) 1996 Wiley-Liss, Inc.
Más información
Título según WOS: | ID WOS:A1996UF55700014 Not found in local WOS DB |
Título de la Revista: | PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS |
Volumen: | 24 |
Número: | 4 |
Editorial: | Wiley |
Fecha de publicación: | 1996 |
Página de inicio: | 523 |
Página final: | 524 |
Notas: | ISI |