artículo
Characterization of crystals of Penicillium purpurogenum acetyl xylan esterase from high-resolution X-ray diffraction
Fecha
1996Registro en:
10.1002/(SICI)1097-0134(199604)24:4<523
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
Institución
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.