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Small angle X‐ray scattering as a complementary tool for high‐throughput structural studies
Author(s) -
Grant Thomas D.,
Luft Joseph R.,
Wolfley Jennifer R.,
Tsuruta Hiro,
Martel Anne,
Montelione Gaetano T.,
Snell Edward H.
Publication year - 2011
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.21630
Subject(s) - small angle x ray scattering , chemistry , crystallography , macromolecule , structural genomics , scattering , resolution (logic) , structural biology , protein structure , physics , computer science , optics , biochemistry , artificial intelligence
Structural crystallography and nuclear magnetic resonance (NMR) spectroscopy are the predominant techniques for understanding the biological world on a molecular level. Crystallography is constrained by the ability to form a crystal that diffracts well and NMR is constrained to smaller proteins. Although powerful techniques, they leave many soluble, purified structurally uncharacterized protein samples. Small angle X‐ray scattering (SAXS) is a solution technique that provides data on the size and multiple conformations of a sample, and can be used to reconstruct a low‐resolution molecular envelope of a macromolecule. In this study, SAXS has been used in a high‐throughput manner on a subset of 28 proteins, where structural information is available from crystallographic and/or NMR techniques. These crystallographic and NMR structures were used to validate the accuracy of molecular envelopes reconstructed from SAXS data on a statistical level, to compare and highlight complementary structural information that SAXS provides, and to leverage biological information derived by crystallographers and spectroscopists from their structures. All the ab initio molecular envelopes calculated from the SAXS data agree well with the available structural information. SAXS is a powerful albeit low‐resolution technique that can provide additional structural information in a high‐throughput and complementary manner to improve the functional interpretation of high‐resolution structures. © 2011 Wiley Periodicals, Inc. Biopolymers 95: 517–530, 2011.