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Small‐angle scattering for structural biology—Expanding the frontier while avoiding the pitfalls

Protein Science · 2010 · Vol. 19(4) · pp. 642–657
David A. JacquesJill Trewhella

Abstract

The last decade has seen a dramatic increase in the use of small-angle scattering for the study of biological macromolecules in solution. The drive for more complete structural characterization of proteins and their interactions, coupled with the increasing availability of instrumentation and easy-to-use software for data analysis and interpretation, is expanding the utility of the technique beyond the domain of the biophysicist and into the realm of the protein scientist. However, the absence of publication standards and the ease with which 3D models can be calculated against the inherently 1D scattering data means that an understanding of sample quality, data quality, and modeling assumptions is essential to have confidence in the results. This review is intended to provide a road map through the small-angle scattering experiment, while also providing a set of guidelines for the critical evaluation of scattering data. Examples of current best practice are given that also demonstrate the power of the technique to advance our understanding of protein structure and function.

Enzyme Structure and FunctionProtein Structure and DynamicsAdvanced NMR Techniques and ApplicationsSmall-angle scatteringScatteringQuality (philosophy)Computer scienceDomain (mathematical analysis)Set (abstract data type)Function (biology)Small-angle X-ray scatteringFrontierInstrumentation (computer programming)

MeSH terms

Models, MolecularProtein ConformationProteinsStructure-Activity RelationshipX-Ray DiffractionScattering, Small Angle

Funding

  • Australian Institute of Nuclear Science and Engineering
Citations
429
FWCI
12.49
field-weighted impact
References
65
Percentile
99%
vs. same field & year
Citations per year
Cited by
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