Document Type
Article
Publication Date
12-2008
Department 1
Physics
Abstract
Modern computing power has made it possible to reconstruct low-resolution, three-dimensional shapes from solution small-angle X-ray scattering (SAXS) data on biomolecules without a priori knowledge of the structure. In conjunction with rapid mixing techniques, SAXS has been applied to time resolve conformational changes accompanying important biological processes, such as biomolecular folding. In response to the widespread interest in SAXS reconstructions, their value in conjunction with such time-resolved data has been examined. The group I intron from Tetrahymena thermophila and its P4–P6 subdomain are ideal model systems for investigation owing to extensive previous studies, including crystal structures. The goal of this paper is to assay the quality of reconstructions from time-resolved data given the sacrifice in signal-to-noise required to obtain sharp time resolution.
Copyright Note
This is the publisher's version of the work. This publication appears in Gettysburg College's institutional repository by permission of the copyright owner for personal use, not for redistribution.
Recommended Citation
Lamb J, Kowk L, Xiangyun Q, Andresen K, Hye Yoon P, Pollack L. Reconstructing three-dimensional shape envelopes from time-resolved small-angle X-ray scattering data. Journal Of Applied Crystallography. December 2008;41(6):1046-1052. http://dx.doi.org/10.1107/S0021889808028264
Required Publisher's Statement
Copyright © International Union of Crystallography
Included in
Atomic, Molecular and Optical Physics Commons, Biological and Chemical Physics Commons, Other Physics Commons