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

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

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