Characterization of crystals of Penicillium purpurogenum acetyl xylan esterase from high-resolution x-ray diffraction.
نویسندگان
چکیده
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.
منابع مشابه
The acetyl xylan esterase II gene from Penicillium purpurogenum is differentially expressed in several carbon sources, and tightly regulated by pH.
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ورودعنوان ژورنال:
- Proteins
دوره 24 4 شماره
صفحات -
تاریخ انتشار 1996