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Methods Enzymol. 2016;579:159-89. doi: 10.1016/bs.mie.2016.05.001. Epub 2016 Jul 1.

Single-Particle Refinement and Variability Analysis in EMAN2.1.

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National Center for Macromolecular Imaging, Baylor College of Medicine, Houston, TX, United States. Electronic address:


CryoEM single-particle reconstruction has been growing rapidly over the last 3 years largely due to the development of direct electron detectors, which have provided data with dramatic improvements in image quality. It is now possible in many cases to produce near-atomic resolution structures, and yet 2/3 of published structures remain at substantially lower resolutions. One important cause for this is compositional and conformational heterogeneity, which is both a resolution-limiting factor and presenting a unique opportunity to better relate structure to function. This manuscript discusses the canonical methods for high-resolution refinement in EMAN2.12, and then considers the wide range of available methods within this package for resolving structural variability, targeting both improved resolution and additional knowledge about particle dynamics.


3-D reconstruction; CryoEM; EMAN; Heterogeneity; Image processing; Motion; Single-particle analysis; Structural biology; Structural variability

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