Journal Article PreJuSER-4375

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High-pressure small-angle neutron scattering studies of glucose isomerase conformation in solution

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2009
Munksgaard Copenhagen

Journal of applied crystallography 42, 461 - 468 () [10.1107/S0021889809007456]

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Abstract: 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.

Keyword(s): J ; scattering standards (auto) ; glucose (auto) ; xylose isomerase (auto) ; structure stability (auto) ; small-angle neutron scattering (SANS) (auto) ; high pressure (auto)

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Note: Partial financial support from the EU NoE SoftComp project (No. S080118) is gratefully acknowledged. This work is based on experiments performed at the Swiss spallation neutron source SINQ, Paul Scherrer Institute, Villigen, Switzerland. We are especially indebted to Dr Ralf Biehl for helpful discussions.

Contributing Institute(s):
  1. Weiche Materie (IFF-7)
Research Program(s):
  1. Kondensierte Materie (P54)

Appears in the scientific report 2009
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