期刊
IUCRJ
卷 3, 期 -, 页码 440-447出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2052252516016018
关键词
small-angle scattering; ab initio modelling; spatial resolution
资金
- EMBL EIPOD programme under Marie Curie COFUND actions
- Bundesministerium fur Bildung and Forschung (BMBF) project BIOSCAT [05K12YE1]
- Horizon 2020 programme of the European Union (iNEXT grant) [653706]
- Biotechnology and Biological Sciences Research Council [BB/M020347/1] Funding Source: researchfish
- BBSRC [BB/M020347/1] Funding Source: UKRI
Spatial resolution is an important characteristic of structural models, and the authors of structures determined by X-ray crystallography or electron cryo-microscopy always provide the resolution upon publication and deposition. Small-angle scattering of X-rays or neutrons (SAS) has recently become a mainstream structural method providing the overall three-dimensional structures of proteins, nucleic acids and complexes in solution. However, no quantitative resolution measure is available for SAS-derived models, which significantly hampers their validation and further use. Here, a method is derived for resolution assessment for ab initio shape reconstruction from scattering data. The inherent variability of the ab initio shapes is utilized and it is demonstrated how their average Fourier shell correlation function is related to the model resolution. The method is validated against simulated data for proteins with known high-resolution structures and its efficiency is demonstrated in applications to experimental data. It is proposed that henceforth the resolution be reported in publications and depositions of ab initio SAS models.
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