discrete heterogeneity
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Author(s):  
Ali Punjani ◽  
David J. Fleet

AbstractSingle 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.


Langmuir ◽  
2015 ◽  
Vol 31 (34) ◽  
pp. 9366-9378 ◽  
Author(s):  
Jacob Trauscht ◽  
Eddy Pazmino ◽  
William P. Johnson

2009 ◽  
Vol 65 (10) ◽  
pp. 1107-1117 ◽  
Author(s):  
Henry van den Bedem ◽  
Ankur Dhanik ◽  
Jean-Claude Latombe ◽  
Ashley M. Deacon

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