CHARACTERIZATION OF CRYSTALS OF PENICILLIUM-PURPUROGENUM ACETYL XYLANESTERASE FROM HIGH-RESOLUTION X-RAY-DIFFRACTION

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 crystal s diffract to better than 1 Angstrom resolution at the Cornell High En ergy Synchrotron Source (CHESS) and are highly stable in the synchrotr on 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 Wil ey-Liss, Inc.