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

作者信息

Pangborn W, Erman M, Li N, Burkhart B M, Pletnev V Z, Duax W L, Gutierrez R, Peirano A, Eyzaguirre J, Thiel D J, Ghosh D

机构信息

Hauptman-Woodward Medical Research Institute, Inc., Buffalo, New York 14203, USA.

出版信息

Proteins. 1996 Apr;24(4):523-4. doi: 10.1002/(SICI)1097-0134(199604)24:4<523::AID-PROT13>3.0.CO;2-N.

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.