title: Preliminary joint X-ray and neutron protein crystallographic studies of endoxylanase II from the fungus Trichoderma longibrachiatum.
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.
authors.affiliation: Bioscience Division, Los Alamos National Laboratory, Los Alamos, NM 87545, USA. ayk@lanl.gov
authors.forename: Andrey Y
authors.initials: AY
authors.lastname: Kovalevsky
authors.forename: B Leif
authors.initials: BL
authors.lastname: Hanson
authors.forename: Sean
authors.initials: S
authors.lastname: Seaver
authors.forename: S Zoë
authors.initials: SZ
authors.lastname: Fisher
authors.forename: Marat
authors.initials: M
authors.lastname: Mustyakimov
authors.forename: Paul
authors.initials: P
authors.lastname: Langan
mesh_terms: D020134:Catalytic Domain; D003461:Crystallography / Q000379:methods; D043364:Endo-1,4-beta Xylanases / Q000737:chemistry*; D005656:Fungal Proteins / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D033363:Neutron Diffraction; D009502:Neutrons; D014242:Trichoderma / Q000201:enzymology*; D014965:X-Rays
chemical_list: D005656:Fungal Proteins; D043364:Endo-1,4-beta Xylanases