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Crystallization and preliminary X-ray diffraction studies of the catalytic core of acetyl xylan esterase from Trichoderma reesei

  • Nina Hakulinen
  • , Maija Tenkanen
  • , Juha Rouvinen*
  • *Corresponding author for this work
  • University of Eastern Finland

Research output: Contribution to journalArticleScientificpeer-review

Abstract

Acetyl xylan esterase is involved in the biodegradation of hemicellulose. It cleaves O-acetyl groups from xylan, which is the most abundant hemicellulose in nature. The catalytic core of acetyl xylan esterase from T. reesei has been crystallized and X-ray diffraction data at 2.3 Å collected. The crystal belongs to the triclinic space group P1 with unit-cell parameters a = 50.3, b = 62.1, c = 40.0 Å, α = 110.1, β = 113.6 and γ = 97.9°. The asymmetric unit contains two molecules.
Original languageEnglish
Pages (from-to)430-432
JournalActa Crystallographica Section D: Biological Crystallography
Volume54
Issue number3
DOIs
Publication statusPublished - 1998
MoE publication typeA1 Journal article-refereed

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