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- W3131760520 endingPage "107702" @default.
- W3131760520 startingPage "107702" @default.
- W3131760520 abstract "Single particle cryo-EM excels in determining static structures of protein molecules, but existing 3D reconstruction methods have been ineffective in modelling flexible proteins. We introduce 3D variability analysis (3DVA), an algorithm that fits a linear subspace model of conformational change to cryo-EM data at high resolution. 3DVA enables the resolution and visualization of detailed molecular motions of both large and small proteins, revealing new biological insight from single particle cryo-EM data. Experimental results demonstrate the ability of 3DVA to resolve multiple flexible motions of α-helices in the sub-50 kDa transmembrane domain of a GPCR complex, bending modes of a sodium ion channel, five types of symmetric and symmetry-breaking flexibility in a proteasome, large motions in a spliceosome complex, and discrete conformational states of a ribosome assembly. 3DVA is implemented in the cryoSPARC software package." @default.
- W3131760520 created "2021-03-01" @default.
- W3131760520 creator A5032901680 @default.
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- W3131760520 date "2021-06-01" @default.
- W3131760520 modified "2023-10-10" @default.
- W3131760520 title "3D variability analysis: Resolving continuous flexibility and discrete heterogeneity from single particle cryo-EM" @default.
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- W3131760520 doi "https://doi.org/10.1016/j.jsb.2021.107702" @default.
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