Mapping the motion and structure of flexible proteins from cryo-em data

Mapping the motion and structure of flexible proteins from cryo-em data

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A deep learning algorithm maps out the continuous conformational changes of flexible protein molecules from single-particle cryo-electron microscopy images, allowing the visualization of the


conformational landscape of a protein with improved resolution of its moving parts. Access through your institution Buy or subscribe This is a preview of subscription content, access via


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subscriptions * Read our FAQs * Contact customer support REFERENCES * Lyumkis, D. Challenges and opportunities in cryo-EM single-particle analysis. _Biol. Chem._ 29, 5181–5197 (2019). THIS


REVIEW ARTICLE PROVIDES AN OVERVIEW OF SINGLE-PARTICLE CRYO-EM FUNDAMENTALS AND THE IMPORTANCE OF MAPPING OUT CONFORMATIONAL HETEROGENEITY. Article  Google Scholar  * Punjani, A. &


Fleet, D. J. 3D Variability analysis: directly resolving continuous flexibility and discrete heterogeneity from single particle cryo-EM images. _J. Struct. Biol._ 213, 107702 (2021). THIS


PAPER REPORTS A COMPUTATIONAL METHOD FOR FITTING A LINEAR SUBSPACE MODEL OF CRYO-EM DENSITY TO SINGLE PARTICLE DATA AND IS AN IMPORTANT BASELINE FOR METHODS THAT RESOLVE CONTINUOUS


HETEROGENEITY. Article  CAS  PubMed  Google Scholar  * Zhong, E. D., Bepler, T., Berger, B. & Davis, J. H. CryoDRGN: reconstruction of heterogeneous cryo-EM structures using neural


networks. _Nat. Methods_ 18, 176–185 (2021). THIS ARTICLE REPORTS A DEEP GENERATIVE MODEL OF CRYO-EM DENSITY MAPS THAT CAN EFFECTIVELY MAP OUT NON-LINEAR CHANGES ACROSS A CONFORMATIONAL


LANDSCAPE. Article  CAS  PubMed  PubMed Central  Google Scholar  * Chen, M. & Ludtke, S. J. Deep learning-based mixed-dimensional Gaussian mixture model for characterizing variability in


cryo-EM. _Nat. Methods_ 18, 930–936 (2021). THIS PAPER REPORTS A DEEP GENERATIVE MODEL THAT CAN REPRESENT THE MOTION OF PARTICLE DENSITY USING THE DISPLACEMENT OF GAUSSIAN MIXTURE


COMPONENTS. Article  CAS  PubMed  PubMed Central  Google Scholar  * Punjani, A., Rubinstein, J. L., Fleet, D. J. & Brubaker, M. A. CryoSPARC: Algorithms for rapid unsupervised cryo-EM


structure determination. _Nat. Methods_ 14, 290–296 (2017). THIS ARTICLE REPORTS THE DEVELOPMENT OF THE CRYOSPARC SOFTWARE SYSTEM, IN WHICH 3DFLEX IS IMPLEMENTED. Article  CAS  PubMed 


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affiliations. THIS IS A SUMMARY OF: Punjani, A. & Fleet, D. J. 3DFlex: determining structure and motion of flexible proteins from cryo-EM. _Nat. Methods_


https://doi.org/10.1038/s41592-023-01853-8 (2023). RIGHTS AND PERMISSIONS Reprints and permissions ABOUT THIS ARTICLE CITE THIS ARTICLE Mapping the motion and structure of flexible proteins


from cryo-EM data. _Nat Methods_ 20, 797–798 (2023). https://doi.org/10.1038/s41592-023-01883-2 Download citation * Published: 12 May 2023 * Issue Date: June 2023 * DOI:


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