{"entity": "researcher", "timestamp": "2026-07-11T14:19:15.329Z", "family": "H\u00f6gbom", "given": "Martin", "initials": "M", "orcid": "0000-0001-5574-9383", "affiliations": ["Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden. hogbom@dbb.su.se."], "links": {"self": {"href": "https://publications.scilifelab.se/researcher/d968fcccace74b689185bb9fa2d33bf8.json"}, "display": {"href": "https://publications.scilifelab.se/researcher/d968fcccace74b689185bb9fa2d33bf8"}}, "publications": [{"entity": "publication", "iuid": "87ba0d1a6c6c409db86213933d82eaeb", "links": {"self": {"href": "https://publications.scilifelab.se/publication/87ba0d1a6c6c409db86213933d82eaeb.json"}, "display": {"href": "https://publications.scilifelab.se/publication/87ba0d1a6c6c409db86213933d82eaeb"}}, "title": "Inhibition mechanism of potential antituberculosis compound lansoprazole sulfide.", "authors": [{"family": "Kovalova", "given": "Terezia", "initials": "T", "orcid": "0000-0002-0144-2463", "researcher": {"href": "https://publications.scilifelab.se/researcher/28a04987c43944d788c125a1dfd15828.json"}}, {"family": "Kr\u00f3l", "given": "Sylwia", "initials": "S"}, {"family": "Gamiz-Hernandez", "given": "Ana P", "initials": "AP", "orcid": "0000-0002-0961-328X", "researcher": {"href": "https://publications.scilifelab.se/researcher/8021ee901c9442e792bba76d38984d4a.json"}}, {"family": "Sj\u00f6strand", "given": "Dan", "initials": "D"}, {"family": "Kaila", "given": "Ville R I", "initials": "VRI", "orcid": "0000-0003-4464-6324", "researcher": {"href": "https://publications.scilifelab.se/researcher/cdcc63256cea406c9cb9cdaecc9cbcbe.json"}}, {"family": "Brzezinski", "given": "Peter", "initials": "P", "orcid": "0000-0003-3860-4988", "researcher": {"href": "https://publications.scilifelab.se/researcher/e3314030ecf94791a713a068d4926c20.json"}}, {"family": "H\u00f6gbom", "given": "Martin", "initials": "M", "orcid": "0000-0001-5574-9383", "researcher": {"href": "https://publications.scilifelab.se/researcher/d968fcccace74b689185bb9fa2d33bf8.json"}}], "type": "journal article", "published": "2024-11-19", "journal": {"title": "Proc. Natl. Acad. Sci. U.S.A.", "issn": "1091-6490", "volume": "121", "issue": "47", "pages": "e2412780121", "issn-l": "0027-8424"}, "abstract": "Tuberculosis is one of the most common causes of death worldwide, with a rapid emergence of multi-drug-resistant strains underscoring the need for new antituberculosis drugs. Recent studies indicate that lansoprazole-a known gastric proton pump inhibitor and its intracellular metabolite, lansoprazole sulfide (LPZS)-are potential antituberculosis compounds. Yet, their inhibitory mechanism and site of action still remain unknown. Here, we combine biochemical, computational, and structural approaches to probe the interaction of LPZS with the respiratory chain supercomplex III2IV2 of Mycobacterium smegmatis, a close homolog of Mycobacterium tuberculosis supercomplex. We show that LPZS binds to the Qo cavity of the mycobacterial supercomplex, inhibiting the quinol substrate oxidation process and the activity of the enzyme. We solve high-resolution (2.6 \u00c5) cryo-electron microscopy (cryo-EM) structures of the supercomplex with bound LPZS that together with microsecond molecular dynamics simulations, directed mutagenesis, and functional assays reveal key interactions that stabilize the inhibitor, but also how mutations can lead to the emergence of drug resistance. Our combined findings reveal an inhibitory mechanism of LPZS and provide a structural basis for drug development against tuberculosis.", "doi": "10.1073/pnas.2412780121", "pmid": "39531492", "labels": {"Cryo-EM": "Service"}, "xrefs": [{"db": "pmc", "key": "PMC11588064"}], "notes": [], "created": "2024-11-15T08:52:59.415Z", "modified": "2025-11-25T15:59:03.981Z"}, {"entity": "publication", "iuid": "88d3b144a82242fe917650dbb2327d3d", "links": {"self": {"href": "https://publications.scilifelab.se/publication/88d3b144a82242fe917650dbb2327d3d.json"}, "display": {"href": "https://publications.scilifelab.se/publication/88d3b144a82242fe917650dbb2327d3d"}}, "title": "Long-range charge transfer mechanism of the III2IV2 mycobacterial supercomplex.", "authors": [{"family": "Riepl", "given": "Daniel", "initials": "D", "orcid": "0000-0002-5641-3037", "researcher": {"href": "https://publications.scilifelab.se/researcher/9d319a620085414b92d1b92fb640ec72.json"}}, {"family": "Gamiz-Hernandez", "given": "Ana P", "initials": "AP", "orcid": "0000-0002-0961-328X", "researcher": {"href": "https://publications.scilifelab.se/researcher/8021ee901c9442e792bba76d38984d4a.json"}}, {"family": "Kovalova", "given": "Terezia", "initials": "T", "orcid": "0000-0002-0144-2463", "researcher": {"href": "https://publications.scilifelab.se/researcher/28a04987c43944d788c125a1dfd15828.json"}}, {"family": "Kr\u00f3l", "given": "Sylwia M", "initials": "SM"}, {"family": "Mader", "given": "Sophie L", "initials": "SL", "orcid": "0000-0002-3011-3319", "researcher": {"href": "https://publications.scilifelab.se/researcher/23c686122cd34cfe9a4ab53c925c246d.json"}}, {"family": "Sj\u00f6strand", "given": "Dan", "initials": "D"}, {"family": "H\u00f6gbom", "given": "Martin", "initials": "M", "orcid": "0000-0001-5574-9383", "researcher": {"href": "https://publications.scilifelab.se/researcher/d968fcccace74b689185bb9fa2d33bf8.json"}}, {"family": "Brzezinski", "given": "Peter", "initials": "P", "orcid": "0000-0003-3860-4988", "researcher": {"href": "https://publications.scilifelab.se/researcher/e3314030ecf94791a713a068d4926c20.json"}}, {"family": "Kaila", "given": "Ville R I", "initials": "VRI", "orcid": "0000-0003-4464-6324", "researcher": {"href": "https://publications.scilifelab.se/researcher/cdcc63256cea406c9cb9cdaecc9cbcbe.json"}}], "type": "journal article", "published": "2024-06-20", "journal": {"title": "Nat Commun", "issn": "2041-1723", "volume": "15", "issue": "1", "pages": "5276", "issn-l": "2041-1723"}, "abstract": "Aerobic life is powered by membrane-bound redox enzymes that shuttle electrons to oxygen and transfer protons across a biological membrane. Structural studies suggest that these energy-transducing enzymes operate as higher-order supercomplexes, but their functional role remains poorly understood and highly debated. Here we resolve the functional dynamics of the 0.7 MDa III2IV2 obligate supercomplex from Mycobacterium smegmatis, a close relative of M. tuberculosis, the causative agent of tuberculosis. By combining computational, biochemical, and high-resolution (2.3 \u00c5) cryo-electron microscopy experiments, we show how the mycobacterial supercomplex catalyses long-range charge transport from its menaquinol oxidation site to the binuclear active site for oxygen reduction. Our data reveal proton and electron pathways responsible for the charge transfer reactions, mechanistic principles of the quinone catalysis, and how unique molecular adaptations, water molecules, and lipid interactions enable the proton-coupled electron transfer (PCET) reactions. Our combined findings provide a mechanistic blueprint of mycobacterial supercomplexes and a basis for developing drugs against pathogenic bacteria.", "doi": "10.1038/s41467-024-49628-9", "pmid": "38902248", "labels": {"Cryo-EM": "Service"}, "xrefs": [{"db": "pmc", "key": "PMC11189923"}, {"db": "pii", "key": "10.1038/s41467-024-49628-9"}], "notes": [], "created": "2024-11-15T08:56:46.121Z", "modified": "2024-11-15T10:41:20.395Z"}, {"entity": "publication", "iuid": "8ccb2185171e4920aba5fe4a63acd358", "links": {"self": {"href": "https://publications.scilifelab.se/publication/8ccb2185171e4920aba5fe4a63acd358.json"}, "display": {"href": "https://publications.scilifelab.se/publication/8ccb2185171e4920aba5fe4a63acd358"}}, "title": "Alternating L4 loop architecture of the bacterial polysaccharide co-polymerase WzzE.", "authors": [{"family": "Wiseman", "given": "Benjamin", "initials": "B", "orcid": "0000-0002-2994-5839", "researcher": {"href": "https://publications.scilifelab.se/researcher/2098646fa9de4dbc8f7cca8aeabad319.json"}}, {"family": "Widmalm", "given": "G\u00f6ran", "initials": "G", "orcid": "0000-0001-8303-4481", "researcher": {"href": "https://publications.scilifelab.se/researcher/7eb393e8ba544f67b39fd6571b4e6efc.json"}}, {"family": "H\u00f6gbom", "given": "Martin", "initials": "M", "orcid": "0000-0001-5574-9383", "researcher": {"href": "https://publications.scilifelab.se/researcher/d968fcccace74b689185bb9fa2d33bf8.json"}}], "type": "journal article", "published": "2023-08-02", "journal": {"title": "Commun Biol", "issn": "2399-3642", "volume": "6", "issue": "1", "pages": "802", "issn-l": "2399-3642"}, "abstract": "Lipopolysaccharides such as the enterobacterial common antigen are important components of the enterobacterial cell envelope that act as a protective barrier against the environment and are often polymerized by the inner membrane bound Wzy-dependent pathway. By employing cryo-electron microscopy we show that WzzE, the co-polymerase component of this pathway that is responsible for the length modulation of the enterobacterial common antigen, is octameric with alternating up-down conformations of its L4 loops. The alternating up-down nature of these essential loops, located at the top of the periplasmic bell, are modulated by clashing helical faces between adjacent protomers that flank the L4 loops around the octameric periplasmic bell. This alternating arrangement and a highly negatively charged binding face create a dynamic environment in which the polysaccharide chain is extended, and suggest a ratchet-type mechanism for polysaccharide elongation.", "doi": "10.1038/s42003-023-05157-7", "pmid": "37532793", "labels": {"Cryo-EM": "Service"}, "xrefs": [{"db": "pmc", "key": "PMC10397196"}, {"db": "pii", "key": "10.1038/s42003-023-05157-7"}], "notes": [], "created": "2023-08-15T12:44:22.734Z", "modified": "2023-11-24T18:13:09.485Z"}, {"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": "84dc535b12fa4c0198fd8f04cf4b2644", "links": {"self": {"href": "https://publications.scilifelab.se/publication/84dc535b12fa4c0198fd8f04cf4b2644.json"}, "display": {"href": "https://publications.scilifelab.se/publication/84dc535b12fa4c0198fd8f04cf4b2644"}}, "title": "The respiratory supercomplex from C. glutamicum.", "authors": [{"family": "Moe", "given": "Agnes", "initials": "A", "orcid": "0000-0002-3328-763X", "researcher": {"href": "https://publications.scilifelab.se/researcher/1cf8d942c69c45c9b72872f0803d0c78.json"}}, {"family": "Kovalova", "given": "Terezia", "initials": "T", "orcid": "0000-0002-0144-2463", "researcher": {"href": "https://publications.scilifelab.se/researcher/28a04987c43944d788c125a1dfd15828.json"}}, {"family": "Kr\u00f3l", "given": "Sylwia", "initials": "S"}, {"family": "Yanofsky", "given": "David J", "initials": "DJ"}, {"family": "Bott", "given": "Michael", "initials": "M"}, {"family": "Sj\u00f6strand", "given": "Dan", "initials": "D"}, {"family": "Rubinstein", "given": "John L", "initials": "JL", "orcid": "0000-0003-0566-2209", "researcher": {"href": "https://publications.scilifelab.se/researcher/771d163fc4b543669ee8fd1148bfe24d.json"}}, {"family": "H\u00f6gbom", "given": "Martin", "initials": "M", "orcid": "0000-0001-5574-9383", "researcher": {"href": "https://publications.scilifelab.se/researcher/d968fcccace74b689185bb9fa2d33bf8.json"}}, {"family": "Brzezinski", "given": "Peter", "initials": "P", "orcid": "0000-0003-3860-4988", "researcher": {"href": "https://publications.scilifelab.se/researcher/e3314030ecf94791a713a068d4926c20.json"}}], "type": "journal article", "published": "2022-03-03", "journal": {"title": "Structure", "issn": "1878-4186", "volume": "30", "issue": "3", "pages": "338-349.e3", "issn-l": "0969-2126"}, "abstract": "Corynebacterium glutamicum is a preferentially aerobic gram-positive bacterium belonging to the phylum Actinobacteria, which also includes the pathogen Mycobacterium tuberculosis. In these bacteria, respiratory complexes III and IV form a CIII2CIV2 supercomplex that catalyzes oxidation of menaquinol and reduction of dioxygen to water. We isolated the C. glutamicum supercomplex and used cryo-EM to determine its structure at 2.9 \u00c5 resolution. The structure shows a central CIII2 dimer flanked by a CIV on two sides. A menaquinone is bound in each of the QN and QP sites in each CIII and an additional menaquinone is positioned \u223c14 \u00c5 from heme bL. A di-heme cyt. cc subunit electronically connects each CIII with an adjacent CIV, with the Rieske iron-sulfur protein positioned with the iron near heme bL. Multiple subunits interact to form a convoluted sub-structure at the cytoplasmic side of the supercomplex, which defines a path for proton transfer into CIV.", "doi": "10.1016/j.str.2021.11.008", "pmid": "34910901", "labels": {"Cryo-EM": "Service"}, "xrefs": [{"db": "pii", "key": "S0969-2126(21)00420-2"}], "notes": [], "created": "2022-03-22T10:03:37.876Z", "modified": "2024-11-15T08:54:18.217Z"}, {"entity": "publication", "iuid": "fc11fc0561274cad8b75a6b4042e1ae4", "links": {"self": {"href": "https://publications.scilifelab.se/publication/fc11fc0561274cad8b75a6b4042e1ae4.json"}, "display": {"href": "https://publications.scilifelab.se/publication/fc11fc0561274cad8b75a6b4042e1ae4"}}, "title": "Substrate-bound and substrate-free outward-facing structures of a multidrug ABC exporter.", "authors": [{"family": "Chaptal", "given": "Vincent", "initials": "V", "orcid": "0000-0003-2603-0294", "researcher": {"href": "https://publications.scilifelab.se/researcher/417117a3671f42cfaa9d0e6af6962264.json"}}, {"family": "Zampieri", "given": "Veronica", "initials": "V", "orcid": "0000-0002-8292-2951", "researcher": {"href": "https://publications.scilifelab.se/researcher/97d59bc8c12a4244839094cb090fb792.json"}}, {"family": "Wiseman", "given": "Benjamin", "initials": "B", "orcid": "0000-0002-2994-5839", "researcher": {"href": "https://publications.scilifelab.se/researcher/2098646fa9de4dbc8f7cca8aeabad319.json"}}, {"family": "Orelle", "given": "C\u00e9dric", "initials": "C", "orcid": "0000-0003-3418-3290", "researcher": {"href": "https://publications.scilifelab.se/researcher/535f40a445ce4b4ca5f14c3c68bb7695.json"}}, {"family": "Martin", "given": "Juliette", "initials": "J", "orcid": "0000-0002-4787-0885", "researcher": {"href": "https://publications.scilifelab.se/researcher/a0ed31b14b464bb9a733989dc6c026dd.json"}}, {"family": "Nguyen", "given": "Kim-Anh", "initials": "KA", "orcid": "0000-0001-5143-507X", "researcher": {"href": "https://publications.scilifelab.se/researcher/992134f693644a70a6fe03d38bddd3c7.json"}}, {"family": "Gobet", "given": "Alexia", "initials": "A"}, {"family": "Di Cesare", "given": "Margot", "initials": "M", "orcid": "0000-0002-7883-852X", "researcher": {"href": "https://publications.scilifelab.se/researcher/b28e57b6b8104eeea44a290272dffaa4.json"}}, {"family": "Magnard", "given": "Sandrine", "initials": "S", "orcid": "0000-0003-1195-1840", "researcher": {"href": "https://publications.scilifelab.se/researcher/04df653ff50f4bc7ba6d1cf0ae74261e.json"}}, {"family": "Javed", "given": "Waqas", "initials": "W", "orcid": "0000-0002-3381-4794", "researcher": {"href": "https://publications.scilifelab.se/researcher/6a3cbad57a404e269b7d3ecba3ab520a.json"}}, {"family": "Eid", "given": "Jad", "initials": "J"}, {"family": "Kilburg", "given": "Arnaud", "initials": "A", "orcid": "0000-0003-4803-6232", "researcher": {"href": "https://publications.scilifelab.se/researcher/977a2544bc0240a3bf8eb3ccbee19863.json"}}, {"family": "Peuchmaur", "given": "Marine", "initials": "M"}, {"family": "Marcoux", "given": "Julien", "initials": "J", "orcid": "0000-0001-7321-7436", "researcher": {"href": "https://publications.scilifelab.se/researcher/9916769d1e0c43379123c00472e672b6.json"}}, {"family": "Monticelli", "given": "Luca", "initials": "L", "orcid": "0000-0002-6352-4595", "researcher": {"href": "https://publications.scilifelab.se/researcher/3d10f84721bc4214bf9350d0587e1cfc.json"}}, {"family": "Hogbom", "given": "Martin", "initials": "M", "orcid": "0000-0001-5574-9383", "researcher": {"href": "https://publications.scilifelab.se/researcher/d968fcccace74b689185bb9fa2d33bf8.json"}}, {"family": "Schoehn", "given": "Guy", "initials": "G", "orcid": "0000-0002-1459-3201", "researcher": {"href": "https://publications.scilifelab.se/researcher/0df30761c33d4c8db05a3f47f998f93b.json"}}, {"family": "Jault", "given": "Jean-Michel", "initials": "JM", "orcid": "0000-0003-1743-2777", "researcher": {"href": "https://publications.scilifelab.se/researcher/b1a639dd1caf46f2a076c8b10e9e5fea.json"}}, {"family": "Boumendjel", "given": "Ahc\u00e8ne", "initials": "A"}, {"family": "Falson", "given": "Pierre", "initials": "P", "orcid": "0000-0002-9760-4577", "researcher": {"href": "https://publications.scilifelab.se/researcher/f633a18c37cf4cdba35101a956ceb492.json"}}], "type": "journal article", "published": "2022-01-28", "journal": {"title": "Sci Adv", "issn": "2375-2548", "volume": "8", "issue": "4", "pages": "eabg9215", "issn-l": "2375-2548"}, "abstract": "Multidrug ABC transporters translocate drugs across membranes by a mechanism for which the molecular features of drug release are so far unknown. Here, we resolved three ATP-Mg2+-bound outward-facing conformations of the Bacillus subtilis (homodimeric) BmrA by x-ray crystallography and single-particle cryo-electron microscopy (EM) in detergent solution, one of them with rhodamine 6G (R6G), a substrate exported by BmrA when overexpressed in B. subtilis. Two R6G molecules bind to the drug-binding cavity at the level of the outer leaflet, between transmembrane (TM) helices 1-2 of one monomer and TM5'-6' of the other. They induce a rearrangement of TM1-2, highlighting a local flexibility that we confirmed by hydrogen/deuterium exchange and molecular dynamics simulations. In the absence of R6G, simulations show a fast postrelease occlusion of the cavity driven by hydrophobicity, while when present, R6G can move within the cavity, maintaining it open.", "doi": "10.1126/sciadv.abg9215", "pmid": "35080979", "labels": {"Cryo-EM": "Service"}, "xrefs": [{"db": "pmc", "key": "PMC8791611"}], "notes": [], "created": "2022-02-03T21:05:51.843Z", "modified": "2022-12-02T10:10:31.688Z"}, {"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"}, {"entity": "publication", "iuid": "7d5a739243ab4db79f3121bb6574361e", "links": {"self": {"href": "https://publications.scilifelab.se/publication/7d5a739243ab4db79f3121bb6574361e.json"}, "display": {"href": "https://publications.scilifelab.se/publication/7d5a739243ab4db79f3121bb6574361e"}}, "title": "Structure of a full-length bacterial polysaccharide co-polymerase.", "authors": [{"family": "Wiseman", "given": "Benjamin", "initials": "B", "orcid": "0000-0002-2994-5839", "researcher": {"href": "https://publications.scilifelab.se/researcher/2098646fa9de4dbc8f7cca8aeabad319.json"}}, {"family": "Nitharwal", "given": "Ram Gopal", "initials": "RG"}, {"family": "Widmalm", "given": "G\u00f6ran", "initials": "G", "orcid": "0000-0001-8303-4481", "researcher": {"href": "https://publications.scilifelab.se/researcher/7eb393e8ba544f67b39fd6571b4e6efc.json"}}, {"family": "H\u00f6gbom", "given": "Martin", "initials": "M", "orcid": "0000-0001-5574-9383", "researcher": {"href": "https://publications.scilifelab.se/researcher/d968fcccace74b689185bb9fa2d33bf8.json"}}], "type": "journal article", "published": "2021-01-14", "journal": {"title": "Nat Commun", "issn": "2041-1723", "issn-l": "2041-1723", "volume": "12", "issue": "1", "pages": "369"}, "abstract": "Lipopolysaccharides are important components of the bacterial cell envelope that among other things act as a protective barrier against the environment and toxic molecules such as antibiotics. One of the most widely disseminated pathways of polysaccharide biosynthesis is the inner membrane bound Wzy-dependent pathway. Here we present the 3.0 \u00c5 structure of the co-polymerase component of this pathway, WzzB from E. coli solved by single-particle cryo-electron microscopy. The overall architecture is octameric and resembles a box jellyfish containing a large bell-shaped periplasmic domain with the 2-helix transmembrane domain from each protomer, positioned 32 \u00c5 apart, encircling a large empty transmembrane chamber. This structure also reveals the architecture of the transmembrane domain, including the location of key residues for the Wzz-family of proteins and the Wzy-dependent pathway present in many Gram-negative bacteria, explaining several of the previous biochemical and mutational studies and lays the foundation for future investigations.", "doi": "10.1038/s41467-020-20579-1", "pmid": "33446644", "labels": {"Cryo-EM": "Service"}, "xrefs": [{"db": "pii", "key": "10.1038/s41467-020-20579-1"}, {"db": "pmc", "key": "PMC7809406"}], "notes": [], "created": "2021-01-14T16:30:43.331Z", "modified": "2021-12-14T12:33:30.787Z"}, {"entity": "publication", "iuid": "c43fdddf24ee4d548364cd7bb3c5885d", "links": {"self": {"href": "https://publications.scilifelab.se/publication/c43fdddf24ee4d548364cd7bb3c5885d.json"}, "display": {"href": "https://publications.scilifelab.se/publication/c43fdddf24ee4d548364cd7bb3c5885d"}}, "title": "Structure of a functional obligate complex III 2IV2 respiratory supercomplex from Mycobacterium smegmatis.", "authors": [{"family": "Wiseman", "given": "Benjamin", "initials": "B", "orcid": "0000-0002-2994-5839", "researcher": {"href": "https://publications.scilifelab.se/researcher/2098646fa9de4dbc8f7cca8aeabad319.json"}}, {"family": "Nitharwal", "given": "Ram Gopal", "initials": "RG"}, {"family": "Fedotovskaya", "given": "Olga", "initials": "O"}, {"family": "Sch\u00e4fer", "given": "Jacob", "initials": "J"}, {"family": "Guo", "given": "Hui", "initials": "H", "orcid": "0000-0001-7007-2876", "researcher": {"href": "https://publications.scilifelab.se/researcher/f6a0383b19ff4fe78c32a07079f90a51.json"}}, {"family": "Kuang", "given": "Qie", "initials": "Q"}, {"family": "Benlekbir", "given": "Samir", "initials": "S"}, {"family": "Sj\u00f6strand", "given": "Dan", "initials": "D"}, {"family": "\u00c4delroth", "given": "Pia", "initials": "P"}, {"family": "Rubinstein", "given": "John L", "initials": "JL", "orcid": "0000-0003-0566-2209", "researcher": {"href": "https://publications.scilifelab.se/researcher/771d163fc4b543669ee8fd1148bfe24d.json"}}, {"family": "Brzezinski", "given": "Peter", "initials": "P", "orcid": "0000-0003-3860-4988", "researcher": {"href": "https://publications.scilifelab.se/researcher/e3314030ecf94791a713a068d4926c20.json"}}, {"family": "H\u00f6gbom", "given": "Martin", "initials": "M", "orcid": "0000-0001-5574-9383", "researcher": {"href": "https://publications.scilifelab.se/researcher/d968fcccace74b689185bb9fa2d33bf8.json"}}], "type": "journal article", "published": "2018-12-00", "journal": {"title": "Nat. Struct. Mol. Biol.", "issn": "1545-9985", "volume": "25", "issue": "12", "pages": "1128-1136", "issn-l": "1545-9985"}, "abstract": "In the mycobacterial electron-transport chain, respiratory complex III passes electrons from menaquinol to complex IV, which in turn reduces oxygen, the terminal acceptor. Electron transfer is coupled to transmembrane proton translocation, thus establishing the electrochemical proton gradient that drives ATP synthesis. We isolated, biochemically characterized, and determined the structure of the obligate III 2IV2 supercomplex from Mycobacterium smegmatis, a model for Mycobacterium tuberculosis. The supercomplex has quinol:O2 oxidoreductase activity without exogenous cytochrome c and includes a superoxide dismutase subunit that may detoxify reactive oxygen species produced during respiration. We found menaquinone bound in both the Qo and Qi sites of complex III. The complex III-intrinsic diheme cytochrome cc subunit, which functionally replaces both cytochrome c1 and soluble cytochrome c in canonical electron-transport chains, displays two conformations: one in which it provides a direct electronic link to complex IV and another in which it serves as an electrical switch interrupting the connection.", "doi": "10.1038/s41594-018-0160-3", "pmid": "30518849", "labels": {"Cryo-EM": "Service"}, "xrefs": [{"db": "pii", "key": "10.1038/s41594-018-0160-3"}], "notes": [], "created": "2019-08-01T08:29:50.182Z", "modified": "2021-06-21T13:56:08.387Z"}]}