Preliminary joint X-ray and neutron protein crystallographic studies of endoxylanase II from the fungus Trichoderma longibrachiatum

Andrey Y. Kovalevsky, B. Leif Hanson, Sean Seaver, S. Zo Fisher, Marat Mustyakimov, Paul Langan

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

Room-temperature X-ray and neutron diffraction data were measured from a family 11 endoxylanase holoenzyme (XynII) originating from the filamentous fungus Trichoderma longibrachiatum to 1.55 Å resolution using a home source and to 1.80 Å resolution using the Protein Crystallography Station at LANSCE. Crystals of XynII, which is an important enzyme for biofuel production, were grown at pH 8.5 in order to examine the effect of basic conditions on the protonation-state distribution in the active site and throughout the protein molecule and to provide insights for rational engineering of catalytically improved XynII for industrial applications.

Original languageEnglish
Pages (from-to)283-286
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume67
Issue number2
DOIs
StatePublished - Feb 2011
Externally publishedYes

Keywords

  • Biofuels
  • Catalytic mechanism
  • Endoxylanases
  • Glycosidic enzymes
  • Joint X-ray/neutron crystallography
  • Protonation

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