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Robust, High-Throughput Solution Structural Analyses by Small Angle X-Ray Scattering (SAXS)
Nature Methods
  • Greg L. Hura
  • Angeli L. Menon
  • Michal Hammel
  • Robert P. Rambo
  • Farris L. Poole
  • Susan E. Tsutakawa
  • Francis E. Jenney, Philadelphia College of Osteopathic Medicine
  • Scott Classen
  • Kenneth A. Frankel
  • Robert C. Hopkins
  • Sung-Jae Yang
  • Joseph W. Scott
  • Bret D. Dillard
  • Michael W. W. Adams
  • John A. Tainer
Document Type
Article
Publication Date
8-1-2009
Abstract
We present an efficient pipeline enabling high-throughput analysis of protein structure in solution with small angle X-ray scattering (SAXS). Our SAXS pipeline combines automated sample handling of microliter volumes, temperature and anaerobic control, rapid data collection and data analysis, and couples structural analysis with automated archiving. We subjected 50 representative proteins, mostly from Pyrococcus furiosus, to this pipeline and found that 30 were multimeric structures in solution. SAXS analysis allowed us to distinguish aggregated and unfolded proteins, define global structural parameters and oligomeric states for most samples, identify shapes and similar structures for 25 unknown structures, and determine envelopes for 41 proteins. We believe that high-throughput SAXS is an enabling technology that may change the way that structural genomics research is done.
PubMed ID
19620974
Comments

This article was published in Nature Methods, Volume 6, Issue 8, August 2009, Pages 606-12.

The published version is available at http://dx.doi.org/10.1038/nmeth.1353

Copyright © 2009 Nature Publishing Group, a division of Macmillan Publishers Limited

Citation Information
Greg L. Hura, Angeli L. Menon, Michal Hammel, Robert P. Rambo, et al.. "Robust, High-Throughput Solution Structural Analyses by Small Angle X-Ray Scattering (SAXS)" Nature Methods Vol. 6 Iss. 8 (2009) p. 606 - 612
Available at: http://works.bepress.com/francis_jenney/76/