title: Direct comparison of the crystal and solution structure of glucose/xylose isomerase from Streptomyces rubiginosus.
abstract: Glucose isomerase (D-xylose ketol-isomerase, EC 5.3.1.5.) catalyses the isomerization reaction of glucose and xylose. The small angle X-ray scattering (SAXS) data of glucose/xylose isomerase from Streptomyces rubiginosus were recorded for protein solution using synchrotron radiation. The experimental data were compared with theoretical scattering calculated on the basis of the known crystal structure (PDB code: 1OAD). The radius of gyration measured by SAXS (R(G)=3.30 nm) was almost identical and the maximum dimension in the distance distribution function was by about 2.5 % lower than the corresponding values calculated on the basis of the crystal structure.
authors.affiliation: Department of Macromolecular Physics, Faculty of Physics, A. Mickiewicz University, Umultowska 85, 61-614 Poznań, Poland. mkozak@amu.edu.pl
authors.forename: Maciej
authors.initials: M
authors.lastname: Kozak
mesh_terms: D019747:Aldose-Ketose Isomerases / Q000737:chemistry*; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary; D012996:Solutions / Q000737:chemistry; D013302:Streptomyces / Q000201:enzymology*
chemical_list: D012996:Solutions; D019747:Aldose-Ketose Isomerases; C023298:xylose isomerase