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Robust, high-throughput solution structural analyses by small angle x-ray scattering (saxs)

Academic Article
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Overview

authors

  • Hura, G. L.
  • Menon, A. L.
  • Hammel, M.
  • Rambo, R. P.
  • Poole, F. L., 2nd
  • Tsutakawa, S. E.
  • Jenney, F. E., Jr.
  • Classen, S.
  • Frankel, K. A.
  • Hopkins, R. C.
  • Yang, S. J.
  • Scott, J. W.
  • Dillard, B. D.
  • Adams, M. W. W.
  • Tainer, John

publication date

  • August 2009

journal

  • Nature Methods  Journal

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.

subject areas

  • Bacterial Proteins
  • Equipment Design
  • Models, Molecular
  • Protein Conformation
  • Proteins
  • Pyrococcus furiosus
  • Scattering, Small Angle
  • X-Ray Diffraction
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Identity

PubMed Central ID

  • PMC3094553

International Standard Serial Number (ISSN)

  • 1548-7091

Digital Object Identifier (DOI)

  • 10.1038/nmeth.1353

PubMed ID

  • 19620974
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Additional Document Info

start page

  • 606

end page

  • 612

volume

  • 6

issue

  • 8

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