{"entity": "researcher", "timestamp": "2026-08-23T09:27:45.394Z", "family": "Plitzko", "given": "Juergen M", "initials": "JM", "orcid": "0000-0002-6402-8315", "affiliations": ["Max Planck Institute of Biochemistry, Research Group Molecular Structural Biology, Martinsried, Germany.", "Max Planck Institute of Biochemistry, Research Group CryoEM Technology, Martinsried, Germany."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/b6f57f9f827a49649460f9020d1d1ecf.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/b6f57f9f827a49649460f9020d1d1ecf"}}, "publications": [{"entity": "publication", "iuid": "2d25bb662f744affbc213da464d49bf4", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/2d25bb662f744affbc213da464d49bf4.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/2d25bb662f744affbc213da464d49bf4"}}, "title": "Cryo-EM structure of single-layered nucleoprotein-RNA complex from Marburg virus.", "authors": [{"family": "Zinzula", "given": "Luca", "initials": "L", "orcid": "0000-0001-6489-7070", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/d2cab8f15b034e819ef2419f5590a820.json"}}, {"family": "Beck", "given": "Florian", "initials": "F"}, {"family": "Camasta", "given": "Marianna", "initials": "M", "orcid": "0009-0006-3516-9844", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/14fe236d31b64c4e832fc5e48825fed9.json"}}, {"family": "Bohn", "given": "Stefan", "initials": "S", "orcid": "0000-0001-9196-622X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/f8f9db5feac143c38eeb339f3ef98025.json"}}, {"family": "Liu", "given": "Chuan", "initials": "C"}, {"family": "Morado", "given": "Dustin", "initials": "D", "orcid": "0000-0003-4693-3220", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/0afbe6534a6d4f44996fe626924ec1a9.json"}}, {"family": "Bracher", "given": "Andreas", "initials": "A", "orcid": "0000-0001-8530-7594", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/fd933026846442e5aca23f1f1e7e8c56.json"}}, {"family": "Plitzko", "given": "Juergen M", "initials": "JM", "orcid": "0000-0002-6402-8315", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/b6f57f9f827a49649460f9020d1d1ecf.json"}}, {"family": "Baumeister", "given": "Wolfgang", "initials": "W", "orcid": "0000-0001-8154-8809", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/bc41560fa5e6429585744e90733210a5.json"}}], "type": "journal article", "published": "2024-11-27", "journal": {"title": "Nat Commun", "issn": "2041-1723", "volume": "15", "issue": "1", "pages": "10307", "issn-l": "2041-1723"}, "abstract": "Marburg virus (MARV) causes lethal hemorrhagic fever in humans, posing a threat to global health. We determined by cryogenic electron microscopy (cryo-EM) the MARV helical ribonucleoprotein (RNP) complex structure in single-layered conformation, which differs from the previously reported structure of a double-layered helix. Our findings illuminate novel RNP interactions and expand knowledge on MARV genome packaging and nucleocapsid assembly, both processes representing attractive targets for the development of antiviral therapeutics against MARV disease.", "doi": "10.1038/s41467-024-54431-7", "pmid": "39604358", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC11603049"}, {"db": "pii", "key": "10.1038/s41467-024-54431-7"}, {"db": "PDB", "key": "9FVD"}, {"db": "PDB", "key": "5F5M"}, {"db": "PDB", "key": "5F5O"}, {"db": "PDB", "key": "5XSQ"}, {"db": "PDB", "key": "5Z9W"}, {"db": "PDB", "key": "6C54"}, {"db": "PDB", "key": "6NUT"}, {"db": "PDB", "key": "7F1M"}, {"db": "PDB", "key": "7YPW"}, {"db": "PDB", "key": "7YR8"}], "notes": [], "created": "2026-08-21T11:50:00.473Z", "modified": "2026-08-21T11:50:00.796Z"}, {"entity": "publication", "iuid": "0dd2e558a54a42b5bab2709c6c23094a", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/0dd2e558a54a42b5bab2709c6c23094a.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/0dd2e558a54a42b5bab2709c6c23094a"}}, "title": "Serial Lift-Out: sampling the molecular anatomy of whole organisms.", "authors": [{"family": "Schi\u00f8tz", "given": "Oda Helene", "initials": "OH", "orcid": "0009-0008-3301-8270", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/489c35609bbb4daaa9c85d213acaf0e6.json"}}, {"family": "Kaiser", "given": "Christoph J O", "initials": "CJO", "orcid": "0000-0002-8481-6845", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/245e385f68cb4c879700f0acbd4a1145.json"}}, {"family": "Klumpe", "given": "Sven", "initials": "S", "orcid": "0000-0002-8350-6503", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/84f68b26d70542829525169d3263fa5a.json"}}, {"family": "Morado", "given": "Dustin R", "initials": "DR"}, {"family": "Poege", "given": "Matthias", "initials": "M"}, {"family": "Schneider", "given": "Jonathan", "initials": "J"}, {"family": "Beck", "given": "Florian", "initials": "F"}, {"family": "Klebl", "given": "David P", "initials": "DP"}, {"family": "Thompson", "given": "Christopher", "initials": "C"}, {"family": "Plitzko", "given": "J\u00fcrgen M", "initials": "JM", "orcid": "0000-0002-6402-8315", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/b6f57f9f827a49649460f9020d1d1ecf.json"}}], "type": "journal article", "published": "2024-09-00", "journal": {"title": "Nat. Methods", "issn": "1548-7105", "volume": "21", "issue": "9", "pages": "1684-1692", "issn-l": "1548-7091"}, "abstract": "Cryo-focused ion beam milling of frozen-hydrated cells and subsequent cryo-electron tomography (cryo-ET) has enabled the structural elucidation of macromolecular complexes directly inside cells. Application of the technique to multicellular organisms and tissues, however, is still limited by sample preparation. While high-pressure freezing enables the vitrification of thicker samples, it prolongs subsequent preparation due to increased thinning times and the need for extraction procedures. Additionally, thinning removes large portions of the specimen, restricting the imageable volume to the thickness of the final lamella, typically <300 nm. Here we introduce Serial Lift-Out, an enhanced lift-out technique that increases throughput and obtainable contextual information by preparing multiple sections from single transfers. We apply Serial Lift-Out to Caenorhabditis elegans L1 larvae, yielding a cryo-ET dataset sampling the worm's anterior-posterior axis, and resolve its ribosome structure to 7 \u00c5 and a subregion of the 11-protofilament microtubule to 13 \u00c5, illustrating how Serial Lift-Out enables the study of multicellular molecular anatomy.", "doi": "10.1038/s41592-023-02113-5", "pmid": "38110637", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC11399102"}, {"db": "pii", "key": "10.1038/s41592-023-02113-5"}], "notes": [], "created": "2026-08-21T11:52:24.763Z", "modified": "2026-08-21T11:52:24.964Z"}]}