Robust, High-Throughput Solution Structural Analyses by Small Angle X-Ray Scattering (SAXS)
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.
Publication Title
Nature Methods
Volume
6
Issue
8
First Page
606
Last Page
612
PubMed ID
19620974
Recommended Citation
Hura, Greg L.; Menon, Angeli L.; Hammel, Michal; Rambo, Robert P.; Poole, Farris L.; Tsutakawa, Susan E.; Jenney, Francis E.; Classen, Scott; Frankel, Kenneth A.; Hopkins, Robert C.; Yang, Sung-Jae; Scott, Joseph W.; Dillard, Bret D.; Adams, Michael W. W.; and Tainer, John A., "Robust, High-Throughput Solution Structural Analyses by Small Angle X-Ray Scattering (SAXS)" (2009). PCOM Scholarly Works. 57.
https://digitalcommons.pcom.edu/scholarly_papers/57
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