Characterization of crystals of Penicillium purpurogenum acetyl xylan esterase from high-resolution X-ray diffraction
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Date
1996
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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 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.
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Keywords
Esterase, Crystallography, Crystallization, Synchrotron radiation