Robust, high-throughput solution structural analyses by small angle X-ray scattering (SAXS) | Zendy

Greg L. Hura | Zendy; Angeli Lal Me | Zendy; Michal Hammel | Zendy; Robert P. Rambo | Zendy; Farris L. Poole | Zendy; Susan E. Tsutakawa | Zendy; Francis E. Jenney | Zendy; Scott Classen | Zendy; Kenneth A. Frankel | Zendy; Robert C. Hopkins | Zendy; Sung-jae Yang | Zendy; Joseph W. Scott | Zendy; B.D. Dillard | Zendy; Michael W. W. Adams | Zendy; John A. Tainer | Zendy

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Robust, high-throughput solution structural analyses by small angle X-ray scattering (SAXS)

Author(s) -

Greg L. Hura,

Angeli Lal Me,

Michal Hammel,

Robert P. Rambo,

Farris L. Poole,

Susan E. Tsutakawa,

Francis E. Jenney,

Scott Classen,

Kenneth A. Frankel,

Robert C. Hopkins,

Sung-jae Yang,

Joseph W. Scott,

B.D. Dillard,

Michael W. W. Adams,

John A. Tainer

Publication year - 2009

Publication title -

nature methods

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 19.469

H-Index - 318

eISSN - 1548-7105

pISSN - 1548-7091

DOI - 10.1038/nmeth.1353

Subject(s) - small angle x ray scattering , pipeline (software) , throughput , pyrococcus furiosus , structural genomics , scattering , materials science , crystallography , computational biology , biological system , computer science , chemistry , protein structure , physics , biology , optics , biochemistry , gene , archaea , wireless , programming language , telecommunications

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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