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Small‐angle neutron scattering and the errors in protein structures that arise from uncorrected background and intermolecular interactions

Small‐angle neutron scattering and the errors in protein structures that arise from uncorrected... Small‐angle neutron scattering (SANS) provides a unique method to probe soft matter in the 10–100 nm length scale in solutions. In order to determine the shape and size of biological macromolecular structures correctly with SANS, a background‐subtracted, undistorted scattering curve must be measured, and the required accuracy and precision is especially needed at the short‐length‐scale limit. A true scattering curve is also needed to discern whether intermolecular interactions are present, which also are probed in the SANS experiment. This article shows how to detect intermolecular interactions so that subsequent structure modeling can be performed using only data that do not contain such contributions. It is also shown how control of many factors can lead to an accurate baseline, or background, correction for scattering from proteins, especially to account for proton incoherent scattering. Failure to make this background correction properly from proteins, polymers, nucleic acids and lipids can result in incorrect values for the calculated shapes and sizes of the molecules as well as the derived magnitudes of the intermolecular interactions. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Applied Crystallography Wiley

Small‐angle neutron scattering and the errors in protein structures that arise from uncorrected background and intermolecular interactions

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References (24)

Publisher
Wiley
Copyright
Copyright © 2008 Wiley Subscription Services, Inc., A Wiley Company
ISSN
1600-5767
eISSN
1600-5767
DOI
10.1107/S0021889808004950
Publisher site
See Article on Publisher Site

Abstract

Small‐angle neutron scattering (SANS) provides a unique method to probe soft matter in the 10–100 nm length scale in solutions. In order to determine the shape and size of biological macromolecular structures correctly with SANS, a background‐subtracted, undistorted scattering curve must be measured, and the required accuracy and precision is especially needed at the short‐length‐scale limit. A true scattering curve is also needed to discern whether intermolecular interactions are present, which also are probed in the SANS experiment. This article shows how to detect intermolecular interactions so that subsequent structure modeling can be performed using only data that do not contain such contributions. It is also shown how control of many factors can lead to an accurate baseline, or background, correction for scattering from proteins, especially to account for proton incoherent scattering. Failure to make this background correction properly from proteins, polymers, nucleic acids and lipids can result in incorrect values for the calculated shapes and sizes of the molecules as well as the derived magnitudes of the intermolecular interactions.

Journal

Journal of Applied CrystallographyWiley

Published: Apr 1, 2008

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