title: 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 A 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 A, b = 61.0 A, C = 72.5 A.
authors.affiliation: Hauptman-Woodward Medical Research Institute, Inc., Buffalo, New York 14203, USA.
authors.forename: W
authors.initials: W
authors.lastname: Pangborn
authors.forename: M
authors.initials: M
authors.lastname: Erman
authors.forename: N
authors.initials: N
authors.lastname: Li
authors.forename: B M
authors.initials: BM
authors.lastname: Burkhart
authors.forename: V Z
authors.initials: VZ
authors.lastname: Pletnev
authors.forename: W L
authors.initials: WL
authors.lastname: Duax
authors.forename: R
authors.initials: R
authors.lastname: Gutierrez
authors.forename: A
authors.initials: A
authors.lastname: Peirano
authors.forename: J
authors.initials: J
authors.lastname: Eyzaguirre
authors.forename: D J
authors.initials: DJ
authors.lastname: Thiel
authors.forename: D
authors.initials: D
authors.lastname: Ghosh
mesh_terms: D000115:Acetylesterase / Q000737:chemistry*; D010407:Penicillium / Q000201:enzymology*; D014961:X-Ray Diffraction
chemical_list: D000115:Acetylesterase; C081851:acetylxylan esterase