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Reconstructing three-dimensional shape envelopes from time-resolved small-angle X-ray scattering data.

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.

SUBMITTER: Lamb J

PROVIDER: S-EPMC2648657 | biostudies-literature | 2008 Dec

REPOSITORIES: biostudies-literature

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Reconstructing three-dimensional shape envelopes from time-resolved small-angle X-ray scattering data.

Lamb Jessica J Kwok Lisa L Qiu Xiangyun X Andresen Kurt K Park Hye Yoon HY Pollack Lois L

Journal of applied crystallography 20081011 Pt 6

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 ti ...[more]

PMID: 19529835

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