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Characterisation of molecular motions in cryo-EM single-particle data by multi-body refinement in RELION
MRC Lab Mol Biol, Cambridge, England..ORCID iD: 0000-0003-2697-2767
KTH, Centres, SeRC - Swedish e-Science Research Centre. KTH, Centres, Science for Life Laboratory, SciLifeLab. KTH, School of Engineering Sciences (SCI), Physics.ORCID iD: 0000-0002-2734-2794
MRC Lab Mol Biol, Cambridge, England..ORCID iD: 0000-0002-0462-6540
2018 (English)In: eLIFE, E-ISSN 2050-084X, Vol. 7, article id e36861Article in journal (Refereed) Published
Abstract [en]

Macromolecular complexes that exhibit continuous forms of structural flexibility pose a challenge for many existing tools in cryo-EM single-particle analysis. We describe a new tool, called multi-body refinement, which models flexible complexes as a user-defined number of rigid bodies that move independently from each other. Using separate focused refinements with iteratively improved partial signal subtraction, the new tool generates improved reconstructions for each of the defined bodies in a fully automated manner. Moreover, using principal component analysis on the relative orientations of the bodies over all particle images in the data set, we generate movies that describe the most important motions in the data. Our results on two test cases, a cytoplasmic ribosome from Plasmodium falciparum, and the spliceosomal B-complex from yeast, illustrate how multi-body refinement can be useful to gain unique insights into the structure and dynamics of large and flexible macromolecular complexes.

Place, publisher, year, edition, pages
ELIFE SCIENCES PUBLICATIONS LTD , 2018. Vol. 7, article id e36861
National Category
Media Engineering
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URN: urn:nbn:se:kth:diva-231720DOI: 10.7554/eLife.36861ISI: 000435436100001PubMedID: 29856314Scopus ID: 2-s2.0-85051994136OAI: oai:DiVA.org:kth-231720DiVA, id: diva2:1239768
Note

QC 20180817

Available from: 2018-08-17 Created: 2018-08-17 Last updated: 2018-11-13Bibliographically approved

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Lindahl, Erik

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