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

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Vol. 67; no. 2; pp. 283 - 286
• Main Authors: Kovalevsky, Andrey Y., Hanson, B. Leif, Seaver, Sean, Fisher, S. Zoë, Mustyakimov, Marat, Langan, Paul
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01-02-2011; Wiley Subscription Services, Inc
• Subjects: biofuels; Catalytic Domain; catalytic mechanism; Crystallization Communications; Crystallography; Crystallography - methods; Endo-1,4-beta Xylanases - chemistry; endoxylanases; Fungal Proteins - chemistry; Fungi; glycosidic enzymes; Hydrogen-Ion Concentration; joint X-ray/neutron crystallography; Neutron Diffraction; Neutrons; Proteins; protonation; Trichoderma; Trichoderma - enzymology; Trichoderma longibrachiatum; X-Rays
• ISSN: 1744-3091; 1744-3091; 2053-230X
• DOI: 10.1107/S174430911005075X

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.