Characterization of crystals of Penicillium purpurogenum acetyl xylan esterase from high-resolution X-ray diffraction

Pangborn, W; Erman M.; Li, NY; Burkhart, BM; Pletnev, VZ; Duax, WL; Gutierrez, R; Peirano, A; Eyzaguirre, J; Thiel, DJ; Ghosh, D

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