Robust, High-throughput Solution Structural Analyses by Small Angle X-ray Scattering (SAXS)

Overview

Journal Nat Methods

Specialties Biomedical Engineering
Pathology

Date 2009 Jul 22

PMID 19620974

Citations 365

Authors

Greg L Hura

Angeli L Menon

Michal Hammel

Robert P Rambo

Farris L Poole 2nd

Susan E Tsutakawa

Francis E Jenney Jr

Scott Classen

Kenneth A Frankel

Robert C Hopkins

Sung-Jae Yang

Joseph W Scott

Bret D Dillard

Michael W W Adams

John A Tainer

Affiliations

Soon will be listed here.

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.

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