Direct comparison of the crystal and solution structure of xylanase from Trichoderma longibrachiatum.
The small angle X-ray scattering (SAXS) data of xylanase XYNII (endo-1,4-beta-xylan xylanohydrolase EC 3.2.1.8) from Trichoderma longibrachiatum, an enzyme catalysing the reaction of accidental hydrolysis of beta-1,4-D-xylosidic linkages of xylan, were recorded for protein solution using synchrotron radiation. The experimental data were compared with those of theoretical scattering calculated on the basis of the known crystal structure. The radius of gyration measured by SAXS (RG = 1.7 nm) was about 3.5% larger and the maximum dimension in the distance distribution function about 5 % larger than the corresponding values calculated on the basis of the crystal structure.
Kozak
Maciej
M
Department of Macromolecular Physics, Faculty of Physics, A. Mickiewicz University, Poznan, Poland.
D018360:Crystallography, X-Ray; D043364:Endo-1,4-beta Xylanases / Q000737:chemistry*; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D012996:Solutions / Q000737:chemistry; D014242:Trichoderma / Q000201:enzymology*
D012996:Solutions; D043364:Endo-1,4-beta Xylanases