Improved fitting of solution X-ray scattering data to macromolecular structures and structural ensembles by explicit water modeling.

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TitleImproved fitting of solution X-ray scattering data to macromolecular structures and structural ensembles by explicit water modeling.
Publication TypeJournal Article
Year of Publication2010
AuthorsGrishaev, A, Guo, L, Irving, T, Bax, A
JournalJ Am Chem Soc
Volume132
Issue44
Pagination15484-6
Date Published2010 Nov 10
ISSN1520-5126
KeywordsMacromolecular Substances, Models, Molecular, Scattering, Small Angle, Water, X-Rays
Abstract

A new procedure, AXES, is introduced for fitting small-angle X-ray scattering (SAXS) data to macromolecular structures and ensembles of structures. By using explicit water models to account for the effect of solvent, and by restricting the adjustable fitting parameters to those that dominate experimental uncertainties, including sample/buffer rescaling, detector dark current, and, within a narrow range, hydration layer density, superior fits between experimental high resolution structures and SAXS data are obtained. AXES results are found to be more discriminating than standard Crysol fitting of SAXS data when evaluating poorly or incorrectly modeled protein structures. AXES results for ensembles of structures previously generated for ubiquitin show improved fits over fitting of the individual members of these ensembles, indicating these ensembles capture the dynamic behavior of proteins in solution.

DOI10.1021/ja106173n
Alternate JournalJ. Am. Chem. Soc.
PubMed ID20958032
PubMed Central IDPMC2974370
Grant ListP41 GM103622 / GM / NIGMS NIH HHS / United States
P41 RR008630 / RR / NCRR NIH HHS / United States
RR-08630 / RR / NCRR NIH HHS / United States
/ / Intramural NIH HHS / United States