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Cryo-EM uniqueness in structure determination of macromolecular complexes: A selected structural anthology
Stockholm University, Science for Life Laboratory (SciLifeLab). Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.ORCID iD: 0000-0002-3744-9229
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Stockholm University, Science for Life Laboratory (SciLifeLab).ORCID iD: 0000-0002-7697-6427
Number of Authors: 22023 (English)In: Current opinion in structural biology, ISSN 0959-440X, E-ISSN 1879-033X, Vol. 81, article id 102621Article in journal (Refereed) Published
Abstract [en]

Cryogenic electron microscopy (cryo-EM) has become in the past 10 years one of the major tools for the structure determination of proteins. Nowadays, the structure prediction field is experiencing the same revolution and, using AlphaFold2, it is possible to have high-confidence atomic models for virtually any polypeptide chain, smaller than 4000 amino acids, in a simple click. Even in a scenario where all polypeptide chain folding were to be known, cryo-EM retains specific characteristics that make it a unique tool for the structure determination of macromolecular complexes. Using cryo-EM, it is possible to obtain near-atomic structures of large and flexible megacomplexes, describe conformational panoramas, and potentially develop a structural proteomic approach from fully ex vivo specimens.

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2023. Vol. 81, article id 102621
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URN: urn:nbn:se:su:diva-220849DOI: 10.1016/j.sbi.2023.102621ISI: 001030375700001PubMedID: 37315343Scopus ID: 2-s2.0-85161625759OAI: oai:DiVA.org:su-220849DiVA, id: diva2:1796734
Available from: 2023-09-13 Created: 2023-09-13 Last updated: 2023-09-18Bibliographically approved

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Azinas, StavrosCarroni, Marta

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