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

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

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)

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 languageEnglish
Pages (from-to)523-524
Number of pages2
JournalProteins: Structure, Function and Genetics
Volume24
Issue number4
DOIs
Publication statusPublished - 1996

Keywords

  • crystallization
  • crystallography
  • esterase
  • synchrotron radiation

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology

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