Premium
High‐pressure small‐angle neutron scattering studies of glucose isomerase conformation in solution
Author(s) -
Banachowicz Ewa,
Kozak Maciej,
Patkowski Adam,
Meier Gerhard,
Kohlbrecher Joachim
Publication year - 2009
Publication title -
journal of applied crystallography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.429
H-Index - 162
ISSN - 1600-5767
DOI - 10.1107/s0021889809007456
Subject(s) - xylose isomerase , neutron scattering , small angle neutron scattering , chemistry , glucose 6 phosphate isomerase , distortion (music) , neutron diffraction , crystallography , isomerase , thermodynamics , scattering , crystal structure , materials science , enzyme , optics , physics , organic chemistry , amplifier , optoelectronics , cmos
Small‐angle neutron scattering (SANS) of solutions of glucose/xylose isomerase from Streptomyces rubiginosus was measured as a function of pressure. It is shown that the structure of the enzyme in solution as seen by SANS is practically the same as that in the crystal and does not change with pressure up to 150 MPa. This reflects the unusually high structural stability of this material, which makes it extremely interesting to use as a secondary standard for pressure‐dependent SANS experiments. This lack of pressure dependence of the SANS data also indicates that any possible change in hydration of the protein induced by pressure is not visible in the SANS curves. An appropriate correction procedure must be used for the SANS data in order to account for the distortion of the intensity curve due to hard‐sphere and electrostatic interactions. After this correction, the isomerase can be readily used as a secondary standard for SANS measurements.