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

✍ Scribed by Pangborn, Walter; Erman, Mary; Li, Naiyin; Burkhart, Brian M.; Pletnev, Vladimir Z.; Duax, William L.; Gutierrez, Rodrigo; Peirano, Alessandra; Eyzaguirre, Jaime; Thiel, Daniel J.; Ghosh, Debashis

Publisher: John Wiley and Sons
Year: 1996
Tongue: English
Weight: 233 KB
Volume: 24
Category: Article
ISSN: 0887-3585
DOI: 10.1002/(sici)1097-0134(199604)24:4<523::aid-prot13>3.0.co;2-n

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✦ Synopsis

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 P2,2,2' and cell dimensions are a = 34.94 b = 6l.OA, c = 72.5A.

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