{"entity": "researcher", "timestamp": "2026-08-08T15:47:38.161Z", "family": "Lebrette", "given": "Hugo", "initials": "H", "orcid": "0000-0002-8081-181X", "affiliations": ["Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden."], "links": {"self": {"href": "https://publications.scilifelab.se/researcher/17ace145c59b4e8695a5c9b95fe81b92.json"}, "display": {"href": "https://publications.scilifelab.se/researcher/17ace145c59b4e8695a5c9b95fe81b92"}}, "publications": [{"entity": "publication", "iuid": "8d20a817fffa422e9b58fff134f9faef", "links": {"self": {"href": "https://publications.scilifelab.se/publication/8d20a817fffa422e9b58fff134f9faef.json"}, "display": {"href": "https://publications.scilifelab.se/publication/8d20a817fffa422e9b58fff134f9faef"}}, "title": "Comparative structural analysis provides new insights into the function of R2-like ligand-binding oxidase.", "authors": [{"family": "Diamanti", "given": "Riccardo", "initials": "R", "orcid": "0000-0002-9527-9133", "researcher": {"href": "https://publications.scilifelab.se/researcher/7ec5f594c48047af921600dddbfece79.json"}}, {"family": "Srinivas", "given": "Vivek", "initials": "V", "orcid": "0000-0002-0265-1873", "researcher": {"href": "https://publications.scilifelab.se/researcher/a6a2692ce1ff4d07ba13f6a180e9232e.json"}}, {"family": "Johansson", "given": "Annika I", "initials": "AI", "orcid": "0000-0001-5000-1288", "researcher": {"href": "https://publications.scilifelab.se/researcher/0b0835b94db946929c1cb0c8f9319068.json"}}, {"family": "Nordstr\u00f6m", "given": "Anders", "initials": "A", "orcid": "0000-0003-3676-817X", "researcher": {"href": "https://publications.scilifelab.se/researcher/4b1803a3f7624f0d82abd552448bdaed.json"}}, {"family": "Griese", "given": "Julia J", "initials": "JJ", "orcid": "0000-0003-3686-3062", "researcher": {"href": "https://publications.scilifelab.se/researcher/308d2df438d8443ca932fb5111e4590e.json"}}, {"family": "Lebrette", "given": "Hugo", "initials": "H", "orcid": "0000-0002-8081-181X", "researcher": {"href": "https://publications.scilifelab.se/researcher/17ace145c59b4e8695a5c9b95fe81b92.json"}}, {"family": "H\u00f6gbom", "given": "Martin", "initials": "M", "orcid": "0000-0001-5574-9383", "researcher": {"href": "https://publications.scilifelab.se/researcher/d968fcccace74b689185bb9fa2d33bf8.json"}}], "type": "comparative study", "published": "2022-06-00", "journal": {"title": "FEBS Lett.", "issn": "1873-3468", "volume": "596", "issue": "12", "pages": "1600-1610", "issn-l": "0014-5793"}, "abstract": "R2-like ligand-binding oxidase (R2lox) is a ferritin-like protein that harbours a heterodinuclear manganese-iron active site. Although R2lox function is yet to be established, the enzyme binds a fatty acid ligand coordinating the metal centre and catalyses the formation of a tyrosine-valine ether cross-link in the protein scaffold upon O2 activation. Here, we characterized the ligands copurified with R2lox by mass spectrometry-based metabolomics. Moreover, we present the crystal structures of two new homologs of R2lox, from Saccharopolyspora erythraea and Sulfolobus acidocaldarius, at 1.38 \u00c5 and 2.26 \u00c5 resolution, respectively, providing the highest resolution structure for R2lox, as well as new insights into putative mechanisms regulating the function of the enzyme.", "doi": "10.1002/1873-3468.14319", "pmid": "35175627", "labels": {"Swedish Metabolomics Centre": "Collaborative"}, "xrefs": [{"db": "pmc", "key": "PMC9314684"}, {"db": "RefSeq", "key": "WP_011277966"}, {"db": "RefSeq", "key": "WP_009945174"}, {"db": "RefSeq", "key": "yp_148624"}, {"db": "RefSeq", "key": "WP_011278976"}], "notes": [], "created": "2022-12-05T08:09:30.578Z", "modified": "2025-10-17T13:03:14.973Z"}, {"entity": "publication", "iuid": "6c9beebec3bf4e008aa3f11261cfa6e6", "links": {"self": {"href": "https://publications.scilifelab.se/publication/6c9beebec3bf4e008aa3f11261cfa6e6.json"}, "display": {"href": "https://publications.scilifelab.se/publication/6c9beebec3bf4e008aa3f11261cfa6e6"}}, "title": "A simple pressure-assisted method for MicroED specimen preparation.", "authors": [{"family": "Zhao", "given": "Jingjing", "initials": "J", "orcid": "0000-0001-8444-6883", "researcher": {"href": "https://publications.scilifelab.se/researcher/3fbe7f2ca29941ce98c38ca6bf78c534.json"}}, {"family": "Xu", "given": "Hongyi", "initials": "H", "orcid": "0000-0002-8271-3906", "researcher": {"href": "https://publications.scilifelab.se/researcher/f112e6110df1446bbfb2679518da45d8.json"}}, {"family": "Lebrette", "given": "Hugo", "initials": "H", "orcid": "0000-0002-8081-181X", "researcher": {"href": "https://publications.scilifelab.se/researcher/17ace145c59b4e8695a5c9b95fe81b92.json"}}, {"family": "Carroni", "given": "Marta", "initials": "M", "orcid": "0000-0002-7697-6427", "researcher": {"href": "https://publications.scilifelab.se/researcher/e7f1bc1767024368abcb11a83184994a.json"}}, {"family": "Taberman", "given": "Helena", "initials": "H"}, {"family": "H\u00f6gbom", "given": "Martin", "initials": "M", "orcid": "0000-0001-5574-9383", "researcher": {"href": "https://publications.scilifelab.se/researcher/d968fcccace74b689185bb9fa2d33bf8.json"}}, {"family": "Zou", "given": "Xiaodong", "initials": "X", "orcid": "0000-0001-6748-6656", "researcher": {"href": "https://publications.scilifelab.se/researcher/b9bd566204e3499db43d53f2adf626e0.json"}}], "type": "journal article", "published": "2021-08-19", "journal": {"title": "Nat Commun", "issn": "2041-1723", "volume": "12", "issue": "1", "pages": "5036", "issn-l": "2041-1723"}, "abstract": "Micro-crystal electron diffraction (MicroED) has shown great potential for structure determination of macromolecular crystals too small for X-ray diffraction. However, specimen preparation remains a major bottleneck. Here, we report a simple method for preparing MicroED specimens, named Preassis, in which excess liquid is removed through an EM grid with the assistance of pressure. We show the ice thicknesses can be controlled by tuning the pressure in combination with EM grids with appropriate carbon hole sizes. Importantly, Preassis can handle a wide range of protein crystals grown in various buffer conditions including those with high viscosity, as well as samples with low crystal concentrations. Preassis is a simple and universal method for MicroED specimen preparation, and will significantly broaden the applications of MicroED.", "doi": "10.1038/s41467-021-25335-7", "pmid": "34413316", "labels": {"Cryo-EM": "Collaborative"}, "xrefs": [{"db": "pii", "key": "10.1038/s41467-021-25335-7"}, {"db": "pmc", "key": "PMC8377027"}], "notes": [], "created": "2021-12-14T12:47:04.167Z", "modified": "2023-12-04T10:18:11.258Z"}]}