{"entity": "researcher", "timestamp": "2026-07-11T14:23:34.810Z", "family": "Tobiasson", "given": "Victor", "initials": "V", "orcid": "0000-0001-8920-017X", "affiliations": ["Science for Life Laboratory, Department of Biochemistry and Biophysics, Stockholm University, Solna, Sweden."], "links": {"self": {"href": "https://publications.scilifelab.se/researcher/5208789057a94d0d9575476bf9c88d5a.json"}, "display": {"href": "https://publications.scilifelab.se/researcher/5208789057a94d0d9575476bf9c88d5a"}}, "publications": [{"entity": "publication", "iuid": "1c57a97c200a453f883feb3a6b0e660d", "links": {"self": {"href": "https://publications.scilifelab.se/publication/1c57a97c200a453f883feb3a6b0e660d.json"}, "display": {"href": "https://publications.scilifelab.se/publication/1c57a97c200a453f883feb3a6b0e660d"}}, "title": "Numerous rRNA molecules form the apicomplexan mitoribosome via repurposed protein and RNA elements.", "authors": [{"family": "Shikha", "given": "Shikha", "initials": "S", "orcid": "0000-0002-7878-1463", "researcher": {"href": "https://publications.scilifelab.se/researcher/2de6231587194596b907dddf06be1b45.json"}}, {"family": "Tobiasson", "given": "Victor", "initials": "V", "orcid": "0000-0001-8920-017X", "researcher": {"href": "https://publications.scilifelab.se/researcher/5208789057a94d0d9575476bf9c88d5a.json"}}, {"family": "Ferreira Silva", "given": "Mariana", "initials": "M"}, {"family": "Ovciarikova", "given": "Jana", "initials": "J"}, {"family": "Beraldi", "given": "Dario", "initials": "D", "orcid": "0000-0003-1504-5212", "researcher": {"href": "https://publications.scilifelab.se/researcher/2912e8a492a04a1aa8e3dab72e1ed37c.json"}}, {"family": "M\u00fchleip", "given": "Alexander", "initials": "A", "orcid": "0000-0002-1877-2282", "researcher": {"href": "https://publications.scilifelab.se/researcher/921b5acb5b7c402fa06c8c148cbd5340.json"}}, {"family": "Sheiner", "given": "Lilach", "initials": "L", "orcid": "0000-0001-5909-2307", "researcher": {"href": "https://publications.scilifelab.se/researcher/8e426f417f194a75ae9fbc76ea24040e.json"}}], "type": "journal article", "published": "2025-01-18", "journal": {"title": "Nat Commun", "issn": "2041-1723", "volume": "16", "issue": "1", "pages": "817", "issn-l": "2041-1723"}, "abstract": "Mitochondrial ribosomes (mitoribosomes) are essential, and their function of synthesising mitochondrial proteins is universal. The core of almost all mitoribosomes is formed from a small number of long and self-folding rRNA molecules. In contrast, the mitoribosome of the apicomplexan parasite Toxoplasma gondii assembles from over 50 extremely short rRNA molecules. Here, we use cryo-EM to discover the features that enable this unusual mitoribosome to perform its function. We reveal that poly-A tails added to rRNA molecules are integrated into the ribosome, and we demonstrate their essentiality for mitoribosome formation and for parasite survival. This is a distinct function for poly-A tails, which are otherwise known primarily as stabilisers of messenger RNAs. Furthermore, while ribosomes typically consist of unique rRNA sequences, here nine sequences are used twice, each copy integrated in a different mitoribosome domain, revealing one of the mechanisms enabling the extreme mitochondrial genome reduction characteristic to Apicomplexa and to a large group of related microbial eukaryotes. Finally, several transcription factor-like proteins are repurposed to compensate for reduced or lost critical ribosomal domains, including members of the ApiAP2 family thus far considered to be DNA-binding transcription factors.", "doi": "10.1038/s41467-025-56057-9", "pmid": "39827269", "labels": {"Cryo-EM": "Service"}, "xrefs": [{"db": "pmc", "key": "PMC11742926"}, {"db": "pii", "key": "10.1038/s41467-025-56057-9"}], "notes": [], "created": "2025-11-13T09:43:13.776Z", "modified": "2025-11-13T09:43:13.956Z"}, {"entity": "publication", "iuid": "2ad60769fa49433e9865d2124a284a9b", "links": {"self": {"href": "https://publications.scilifelab.se/publication/2ad60769fa49433e9865d2124a284a9b.json"}, "display": {"href": "https://publications.scilifelab.se/publication/2ad60769fa49433e9865d2124a284a9b"}}, "title": "Structure and dynamics of differential ligand binding in the human \u03c1-type GABAA receptor.", "authors": [{"family": "Cowgill", "given": "John", "initials": "J"}, {"family": "Fan", "given": "Chen", "initials": "C"}, {"family": "Haloi", "given": "Nandan", "initials": "N"}, {"family": "Tobiasson", "given": "Victor", "initials": "V", "orcid": "0000-0001-8920-017X", "researcher": {"href": "https://publications.scilifelab.se/researcher/5208789057a94d0d9575476bf9c88d5a.json"}}, {"family": "Zhuang", "given": "Yuxuan", "initials": "Y"}, {"family": "Howard", "given": "Rebecca J", "initials": "RJ"}, {"family": "Lindahl", "given": "Erik", "initials": "E", "orcid": "0000-0003-1333-5398", "researcher": {"href": "https://publications.scilifelab.se/researcher/51600cedcf044bdda0f677deaeaf9fad.json"}}], "type": "journal article", "published": "2023-11-01", "journal": {"title": "Neuron", "issn": "1097-4199", "volume": "111", "issue": "21", "pages": "3450-3464.e5", "issn-l": "0896-6273"}, "abstract": "The neurotransmitter \u03b3-aminobutyric acid (GABA) drives critical inhibitory processes in and beyond the nervous system, partly via ionotropic type-A receptors (GABAARs). Pharmacological properties of \u03c1-type GABAARs are particularly distinctive, yet the structural basis for their specialization remains unclear. Here, we present cryo-EM structures of a lipid-embedded human \u03c11 GABAAR, including a partial intracellular domain, under apo, inhibited, and desensitized conditions. An apparent resting state, determined first in the absence of modulators, was recapitulated with the specific inhibitor (1,2,5,6-tetrahydropyridin-4-yl)methylphosphinic acid and blocker picrotoxin and provided a rationale for bicuculline insensitivity. Comparative structures, mutant recordings, and molecular simulations with and without GABA further explained the sensitized but slower activation of \u03c11 relative to canonical subtypes. Combining GABA with picrotoxin also captured an apparent uncoupled intermediate state. This work reveals structural mechanisms of gating and modulation with applications to \u03c1-specific pharmaceutical design and to our biophysical understanding of ligand-gated ion channels.", "doi": "10.1016/j.neuron.2023.08.006", "pmid": "37659407", "labels": {"Cryo-EM": "Service"}, "xrefs": [{"db": "pii", "key": "S0896-6273(23)00587-1"}], "notes": [], "created": "2023-09-19T08:21:37.127Z", "modified": "2023-12-04T09:50:38.972Z"}, {"entity": "publication", "iuid": "bf067c1c192b4fb5bc57a6b452aa6914", "links": {"self": {"href": "https://publications.scilifelab.se/publication/bf067c1c192b4fb5bc57a6b452aa6914.json"}, "display": {"href": "https://publications.scilifelab.se/publication/bf067c1c192b4fb5bc57a6b452aa6914"}}, "title": "Structural basis of mitochondrial membrane bending by the I-II-III2-IV2 supercomplex.", "authors": [{"family": "M\u00fchleip", "given": "Alexander", "initials": "A", "orcid": "0000-0002-1877-2282", "researcher": {"href": "https://publications.scilifelab.se/researcher/921b5acb5b7c402fa06c8c148cbd5340.json"}}, {"family": "Flygaard", "given": "Rasmus Kock", "initials": "RK", "orcid": "0000-0002-4918-6438", "researcher": {"href": "https://publications.scilifelab.se/researcher/8a5982a29fb44d6b96d84834275b5bd0.json"}}, {"family": "Baradaran", "given": "Rozbeh", "initials": "R", "orcid": "0000-0002-6096-9169", "researcher": {"href": "https://publications.scilifelab.se/researcher/2af7262546e54fc3a36f3bac03e15a79.json"}}, {"family": "Haapanen", "given": "Outi", "initials": "O", "orcid": "0000-0002-1958-8997", "researcher": {"href": "https://publications.scilifelab.se/researcher/8c9485f25724445fb9852e98436beb11.json"}}, {"family": "Gruhl", "given": "Thomas", "initials": "T", "orcid": "0000-0002-6069-1697", "researcher": {"href": "https://publications.scilifelab.se/researcher/ed9d0003c85c46358a2e791f80a71af2.json"}}, {"family": "Tobiasson", "given": "Victor", "initials": "V", "orcid": "0000-0001-8920-017X", "researcher": {"href": "https://publications.scilifelab.se/researcher/5208789057a94d0d9575476bf9c88d5a.json"}}, {"family": "Mar\u00e9chal", "given": "Amandine", "initials": "A", "orcid": "0000-0003-3460-3806", "researcher": {"href": "https://publications.scilifelab.se/researcher/f11686a0d97a4dbba07c816133b76816.json"}}, {"family": "Sharma", "given": "Vivek", "initials": "V", "orcid": "0000-0002-8838-3151", "researcher": {"href": "https://publications.scilifelab.se/researcher/5a6299ddcafc4274940548261eddd42e.json"}}, {"family": "Amunts", "given": "Alexey", "initials": "A", "orcid": "0000-0002-5302-1740", "researcher": {"href": "https://publications.scilifelab.se/researcher/e7d0bf36ad1a47f5b5b88f78d1e15395.json"}}], "type": "journal article", "published": "2023-03-00", "journal": {"title": "Nature", "issn": "1476-4687", "volume": "615", "issue": "7954", "pages": "934-938", "issn-l": "0028-0836"}, "abstract": "Mitochondrial energy conversion requires an intricate architecture of the inner mitochondrial membrane1. Here we show that a supercomplex containing all four respiratory chain components contributes to membrane curvature induction in ciliates. We report cryo-electron microscopy and cryo-tomography structures of the supercomplex that comprises 150 different proteins and 311 bound lipids, forming a stable 5.8-MDa assembly. Owing to subunit acquisition and extension, complex I associates with a complex IV dimer, generating a wedge-shaped gap that serves as a binding site for complex II. Together with a tilted complex III dimer association, it results in a curved membrane region. Using molecular dynamics simulations, we demonstrate that the divergent supercomplex actively contributes to the membrane curvature induction and tubulation of cristae. Our findings highlight how the evolution of protein subunits of respiratory complexes has led to the I-II-III2-IV2 supercomplex that contributes to the shaping of the bioenergetic membrane, thereby enabling its functional specialization.", "doi": "10.1038/s41586-023-05817-y", "pmid": "36949187", "labels": {"Cryo-EM": "Service"}, "xrefs": [{"db": "pmc", "key": "PMC10060162"}, {"db": "pii", "key": "10.1038/s41586-023-05817-y"}], "notes": [], "created": "2023-08-15T12:46:05.104Z", "modified": "2023-12-04T10:01:52.146Z"}, {"entity": "publication", "iuid": "675091121e4145f5934b9aa1f15f6b64", "links": {"self": {"href": "https://publications.scilifelab.se/publication/675091121e4145f5934b9aa1f15f6b64.json"}, "display": {"href": "https://publications.scilifelab.se/publication/675091121e4145f5934b9aa1f15f6b64"}}, "title": "Structure of a mitochondrial ribosome with fragmented rRNA in complex with membrane-targeting elements.", "authors": [{"family": "Tobiasson", "given": "Victor", "initials": "V", "orcid": "0000-0001-8920-017X", "researcher": {"href": "https://publications.scilifelab.se/researcher/5208789057a94d0d9575476bf9c88d5a.json"}}, {"family": "Berzina", "given": "Ieva", "initials": "I", "orcid": "0000-0003-2120-7580", "researcher": {"href": "https://publications.scilifelab.se/researcher/575d868bdeef4e318503564bb8a37e08.json"}}, {"family": "Amunts", "given": "Alexey", "initials": "A", "orcid": "0000-0002-5302-1740", "researcher": {"href": "https://publications.scilifelab.se/researcher/e7d0bf36ad1a47f5b5b88f78d1e15395.json"}}], "type": "journal article", "published": "2022-10-17", "journal": {"title": "Nat Commun", "issn": "2041-1723", "volume": "13", "issue": "1", "pages": "6132", "issn-l": "2041-1723"}, "abstract": "Mitoribosomes of green algae display a great structural divergence from their tracheophyte relatives, with fragmentation of both rRNA and proteins as a defining feature. Here, we report a 2.9 \u00c5 resolution structure of the mitoribosome from the alga Polytomella magna harbouring a reduced rRNA split into 13 fragments. We found that the rRNA contains a non-canonical reduced form of the 5S, as well as a permutation of the LSU domain I. The mt-5S rRNA is stabilised by mL40 that is also found in mitoribosomes lacking the 5S, which suggests an evolutionary pathway. Through comparison to other ribosomes with fragmented rRNAs, we observe that the pattern is shared across large evolutionary distances, and between cellular compartments, indicating an evolutionary convergence and supporting the concept of a primordial fragmented ribosome. On the protein level, eleven peripherally associated HEAT-repeat proteins are involved in the binding of 3' rRNA termini, and the structure features a prominent pseudo-trimer of one of them (mL116). Finally, in the exit tunnel, mL128 constricts the tunnel width of the vestibular area, and mL105, a homolog of a membrane targeting component mediates contacts with an inner membrane bound insertase. Together, the structural analysis provides insight into the evolution of the ribosomal machinery in mitochondria.", "doi": "10.1038/s41467-022-33582-5", "pmid": "36253367", "labels": {"Cryo-EM": "Service"}, "xrefs": [{"db": "pmc", "key": "PMC9576764"}, {"db": "pii", "key": "10.1038/s41467-022-33582-5"}], "notes": [], "created": "2022-11-30T09:55:59.103Z", "modified": "2022-11-30T09:55:59.346Z"}, {"entity": "publication", "iuid": "13b50e6dabb34ef58cf5cc56f7fc51d3", "links": {"self": {"href": "https://publications.scilifelab.se/publication/13b50e6dabb34ef58cf5cc56f7fc51d3.json"}, "display": {"href": "https://publications.scilifelab.se/publication/13b50e6dabb34ef58cf5cc56f7fc51d3"}}, "title": "Type III ATP synthase is a symmetry-deviated dimer that induces membrane curvature through tetramerization.", "authors": [{"family": "Flygaard", "given": "Rasmus Kock", "initials": "RK", "orcid": "0000-0002-4918-6438", "researcher": {"href": "https://publications.scilifelab.se/researcher/8a5982a29fb44d6b96d84834275b5bd0.json"}}, {"family": "M\u00fchleip", "given": "Alexander", "initials": "A", "orcid": "0000-0002-1877-2282", "researcher": {"href": "https://publications.scilifelab.se/researcher/921b5acb5b7c402fa06c8c148cbd5340.json"}}, {"family": "Tobiasson", "given": "Victor", "initials": "V", "orcid": "0000-0001-8920-017X", "researcher": {"href": "https://publications.scilifelab.se/researcher/5208789057a94d0d9575476bf9c88d5a.json"}}, {"family": "Amunts", "given": "Alexey", "initials": "A", "orcid": "0000-0002-5302-1740", "researcher": {"href": "https://publications.scilifelab.se/researcher/e7d0bf36ad1a47f5b5b88f78d1e15395.json"}}], "type": "journal article", "published": "2020-10-22", "journal": {"title": "Nat Commun", "issn": "2041-1723", "volume": "11", "issue": "1", "pages": "5342", "issn-l": "2041-1723"}, "abstract": "Mitochondrial ATP synthases form functional homodimers to induce cristae curvature that is a universal property of mitochondria. To expand on the understanding of this fundamental phenomenon, we characterized the unique type III mitochondrial ATP synthase in its dimeric and tetrameric form. The cryo-EM structure of a ciliate ATP synthase dimer reveals an unusual U-shaped assembly of 81 proteins, including a substoichiometrically bound ATPTT2, 40 lipids, and co-factors NAD and CoQ. A single copy of subunit ATPTT2 functions as a membrane anchor for the dimeric inhibitor IF1. Type III specific linker proteins stably tie the ATP synthase monomers in parallel to each other. The intricate dimer architecture is scaffolded by an extended subunit-a that provides a template for both intra- and inter-dimer interactions. The latter results in the formation of tetramer assemblies, the membrane part of which we determined to 3.1 \u00c5 resolution. The structure of the type III ATP synthase tetramer and its associated lipids suggests that it is the intact unit propagating the membrane curvature.", "doi": "10.1038/s41467-020-18993-6", "pmid": "33093501", "labels": {"Cryo-EM": "Service", "Global Proteomics and Proteogenomics": "Service"}, "xrefs": [{"db": "pii", "key": "10.1038/s41467-020-18993-6"}, {"db": "pmc", "key": "PMC7583250"}], "notes": [], "created": "2020-10-26T14:40:56.262Z", "modified": "2023-12-04T10:09:34.900Z"}, {"entity": "publication", "iuid": "e7a89f61f370498397e2d9bcb024aff8", "links": {"self": {"href": "https://publications.scilifelab.se/publication/e7a89f61f370498397e2d9bcb024aff8.json"}, "display": {"href": "https://publications.scilifelab.se/publication/e7a89f61f370498397e2d9bcb024aff8"}}, "title": "Ciliate mitoribosome illuminates evolutionary steps of mitochondrial translation.", "authors": [{"family": "Tobiasson", "given": "Victor", "initials": "V", "orcid": "0000-0001-8920-017X", "researcher": {"href": "https://publications.scilifelab.se/researcher/5208789057a94d0d9575476bf9c88d5a.json"}}, {"family": "Amunts", "given": "Alexey", "initials": "A", "orcid": "0000-0002-5302-1740", "researcher": {"href": "https://publications.scilifelab.se/researcher/e7d0bf36ad1a47f5b5b88f78d1e15395.json"}}], "type": "journal article", "published": "2020-06-18", "journal": {"volume": "9", "issn": "2050-084X", "issue": null, "pages": "1-15", "title": "Elife", "issn-l": "2050-084X"}, "abstract": "To understand the steps involved in the evolution of translation, we used Tetrahymena thermophila, a ciliate with high coding capacity of the mitochondrial genome, as the model organism and characterized its mitochondrial ribosome (mitoribosome) using cryo-EM. The structure of the mitoribosome reveals an assembly of 94-ribosomal proteins and four-rRNAs with an additional protein mass of ~700 kDa on the small subunit, while the large subunit lacks 5S rRNA. The structure also shows that the small subunit head is constrained, tRNA binding sites are formed by mitochondria-specific protein elements, conserved protein bS1 is excluded, and bacterial RNA polymerase binding site is blocked. We provide evidence for anintrinsic protein targeting system through visualization of mitochondria-specific mL105 by the exit tunnel that would facilitate the recruitment of a nascent polypeptide. Functional protein uS3m is encoded by three complementary genes from the nucleus and mitochondrion, establishing a link between genetic drift and mitochondrial translation. Finally, we reannotated nine open reading frames in the mitochondrial genome that code for mitoribosomal proteins.", "doi": "10.7554/eLife.59264", "pmid": "32553108", "labels": {"Cryo-EM": "Service", "Global Proteomics and Proteogenomics": "Service"}, "xrefs": [{"db": "pii", "key": "59264"}, {"db": "pmc", "key": "PMC7326499"}], "notes": [], "created": "2020-06-20T05:52:44.314Z", "modified": "2021-11-10T12:50:13.521Z"}, {"entity": "publication", "iuid": "7c90ca150f5a41e3ad40f66296f81652", "links": {"self": {"href": "https://publications.scilifelab.se/publication/7c90ca150f5a41e3ad40f66296f81652.json"}, "display": {"href": "https://publications.scilifelab.se/publication/7c90ca150f5a41e3ad40f66296f81652"}}, "title": "Zinc depletion does not necessarily induce ribosome hibernation in mycobacteria.", "authors": [{"family": "Tobiasson", "given": "Victor", "initials": "V", "orcid": "0000-0001-8920-017X", "researcher": {"href": "https://publications.scilifelab.se/researcher/5208789057a94d0d9575476bf9c88d5a.json"}}, {"family": "Dow", "given": "Allexa", "initials": "A"}, {"family": "Prisic", "given": "Sladjana", "initials": "S", "orcid": "0000-0003-3137-4358", "researcher": {"href": "https://publications.scilifelab.se/researcher/57b0ad51d8ec414a8acf3d3886da29d5.json"}}, {"family": "Amunts", "given": "A", "initials": "A", "orcid": "0000-0002-5302-1740", "researcher": {"href": "https://publications.scilifelab.se/researcher/e7d0bf36ad1a47f5b5b88f78d1e15395.json"}}], "type": "letter", "published": "2019-02-12", "journal": {"volume": "116", "issn": "1091-6490", "issue": "7", "pages": "2395-2397", "title": "Proc. Natl. Acad. Sci. U.S.A.", "issn-l": "0027-8424"}, "abstract": null, "doi": "10.1073/pnas.1817490116", "pmid": "30683730", "labels": {"Cryo-EM": "Service"}, "xrefs": [{"db": "pii", "key": "1817490116"}, {"db": "pmc", "key": "PMC6377477"}], "notes": "The cryo-EM data of M. smegmatis Alt ribosomes have been deposited in the Electron Microscopy Data Bank under the accession numbers EMD-0276, EMD0277, EMD-0278, EMD-0284, EMD-0285, and EMD0286", "created": "2019-08-21T10:55:46.969Z", "modified": "2023-12-04T10:13:50.764Z"}, {"entity": "publication", "iuid": "0e147a5dedd845faac46f7a0cdbb4de5", "links": {"self": {"href": "https://publications.scilifelab.se/publication/0e147a5dedd845faac46f7a0cdbb4de5.json"}, "display": {"href": "https://publications.scilifelab.se/publication/0e147a5dedd845faac46f7a0cdbb4de5"}}, "title": "Structure of the chloroplast ribosome with chl-RRF and hibernation-promoting factor", "authors": [{"family": "Perez Boerema", "given": "Annemarie", "initials": "A"}, {"family": "Aibara", "given": "Shintaro", "initials": "S", "orcid": "0000-0003-2221-482X", "researcher": {"href": "https://publications.scilifelab.se/researcher/d66746c4bec5414da78b2a325a13328f.json"}}, {"family": "Paul", "given": "Bijoya", "initials": "B"}, {"family": "Tobiasson", "given": "Victor", "initials": "V", "orcid": "0000-0001-8920-017X", "researcher": {"href": "https://publications.scilifelab.se/researcher/5208789057a94d0d9575476bf9c88d5a.json"}}, {"family": "Kimanius", "given": "Dari", "initials": "D", "orcid": "0000-0002-2662-6373", "researcher": {"href": "https://publications.scilifelab.se/researcher/df2317a49446495a8839262b9f58fe38.json"}}, {"family": "Forsberg", "given": "Bj\u00f6rn O", "initials": "BO", "orcid": "0000-0002-6247-4063", "researcher": {"href": "https://publications.scilifelab.se/researcher/d5434ab128e04b2b951abbbea77221c8.json"}}, {"family": "Wallden", "given": "Karin", "initials": "K"}, {"family": "Lindahl", "given": "Erik", "initials": "E", "orcid": "0000-0003-1333-5398", "researcher": {"href": "https://publications.scilifelab.se/researcher/51600cedcf044bdda0f677deaeaf9fad.json"}}, {"family": "Amunts", "given": "A", "initials": "A", "orcid": "0000-0002-5302-1740", "researcher": {"href": "https://publications.scilifelab.se/researcher/e7d0bf36ad1a47f5b5b88f78d1e15395.json"}}], "type": "journal-article", "published": "2018-04-02", "journal": {"volume": "4", "issn": "2055-0278", "issue": "4", "pages": "212-217", "title": "NPLANTS", "issn-l": "2055-0278"}, "abstract": "Oxygenic photosynthesis produces oxygen and builds a variety of organic compounds, changing the chemistry of the air, the sea and fuelling the food chain on our planet. The photochemical reactions underpinning this process in plants take place in the chloroplast. Chloroplasts evolved ~1.2 billion years ago from an engulfed primordial diazotrophic cyanobacterium, and chlororibosomes are responsible for synthesis of the core proteins driving photochemical reactions. Chlororibosomal activity is spatiotemporally coupled to the synthesis and incorporation of functionally essential co-factors, implying the presence of chloroplast-specific regulatory mechanisms and structural adaptation of the chlororibosome1,2. Despite recent structural information3-6, some of these aspects remained elusive. To provide new insights into the structural specialities and evolution, we report a comprehensive analysis of the 2.9-3.1 \u00c5 resolution electron cryo-microscopy structure of the spinach chlororibosome in complex with its recycling factor and hibernation-promoting factor. The model reveals a prominent channel extending from the exit tunnel to the chlororibosome exterior, structural re-arrangements that lead to increased surface area for translocon binding, and experimental evidence for parallel and convergent evolution of chloro- and mitoribosomes.", "doi": "10.1038/s41477-018-0129-6", "pmid": "29610536", "labels": {"Cryo-EM": "Service"}, "xrefs": [{"db": "pii", "key": "10.1038/s41477-018-0129-6"}], "notes": [], "created": "2018-04-11T08:19:19.613Z", "modified": "2023-12-04T10:12:49.407Z"}]}