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 = 34.9Å, b = 61.0Å, c = 72.5Å.
Original language | English |
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Pages (from-to) | 523-524 |
Number of pages | 2 |
Journal | Proteins: Structure, Function and Genetics |
Volume | 24 |
Issue number | 4 |
DOIs | |
Publication status | Published - 1996 |
Keywords
- crystallization
- crystallography
- esterase
- synchrotron radiation
ASJC Scopus subject areas
- Structural Biology
- Biochemistry
- Molecular Biology