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Lista publikacji - Narodowe Centrum Promieniowania Synchrotronowego SOLARIS

Cryo-EM

CRYO-EM - lista publikacji

Zachęcamy do zapoznania się z listą wszystkich publikacji naukowych Centrum SOLARIS. Lista dostępna po kliknięciu w aktywny link.

Lista publikacji będąca wynikiem badań zrealizowanych na CRYO-EM:

2026

  1. G. Ważny, M. Jaciuk, P. Indyka, S. Glatt, A. Biela, M. Rawski, Influence of total electron dose on the quality of nucleic acids potential maps in Cryo-EM, Ultramicroscopy 283, 114358, 2026, DOI: 10.1016/j.ultramic.2026.114358
  2. Łukasz Koziej, Jędrzej Pankowski, Monika Stefańska, Daniel Jankowski, Agnieszka Gawin, V. Vishal Malolan, Juha T. Huiskonen, Takahiro Kosugi, Yusuke Azuma, A molecular basis for stoichiometric enzyme encapsulation in the vitamin B2 biosynthesis compartment, Nature Communications 2026, DOI:10.1038/s41467-026-73260-4
  3. Piotr Stepien, Gerrit Wilkens, Sylwia Swiatek, Manuel Yusef Robles, Anna Swietlikowska, Sarah Hutchings, Dmitry Ghilarov, Jonathan G. Heddle, Precise Capture of Membrane Proteins Using DNA-Origami-Constrained Nanodiscs, Small structures, 2026, DOI: 10.1002/sstr.202500688

  4. G Ważny, P Indyka, M Rawski, M Jaciuk, A Biela, Cryo-EM Facility at SOLARIS - A Highlight Review of Complex Biological Assemblies, Acta Physica Polonica: A 149 (5), S167, (2026), doi: 10.12693/APhysPolA.149.S167 

  5. E. Warmbier-Wytykowska, M. Radiom, P. Wagner, S. Różańska, P. Fischer, J. Różański, Alkyl polyglucoside–based viscoelastic systems: roles of anionic surfactant, salts, and metal chelates, Journal of Molecular Liquids, Volume 456,( 2026), 129655, doi: 10.1016/j.molliq.2026.129655

  6. T. W. Ettema, S. Inaba-Inoue, c. Thangaratnarajah , L. Alves da Silva , N. Senning, A. Clarke, P. Stepien, A. Shah, Y. Ma ,K.  Hardman , S. David , H. El Mkami , JG. Heddle,  N. Nomura, S. Ogasawara, S. Iwata, D. Ghilarov, C. Pliotas , T.  Stockner,  D. J. Slotboom, K. Beis,  Shared structural mechanisms of alternating access between the secondary peptide transporter SbmA and ABC transporters, Nature Communications, 15;17(1):5619, (2026), doi: 10.1038/s41467-026-71633-3

  7. M. Wytrwal, E. Oclon, S. Rzepa, L. Pardyak, K. Filipek, M. Kucharski, M. Górniewicz-Lorens, K. Szczubiałka, Kartogenin-loaded liposomes coated with alkylated hyaluronic acid for stimulated chondrogenic differentiation, International Journal of Pharmaceutics, 701,127167, (2026), doi.org/10.1016/j.ijpharm.2026.127167

  8. F. Santamaria, I. Gugel, V.  Dzyhovskyi, P. Moretti, P. Mariani, A. Pepe, M. G. Ortore, M. Rawski,
    A. Baldisserotto, S. Manfredini, A. Casoni, M. Benedusi, G. Valacchi, E. Esposito, (2026), Design and characterization of a Transethosome‐Based gel for cutaneous administration of genistein, Journal of Nanotechnology, (1), 16, (2026), doi: org/10.1155/jnt/3911170

  9. S. Dutt, L. B. Lai, R.  Mehta, B. I. Karawdeniya, Y. M. Nuwan D Y Bandara, A. J. Clulow, S. Glatt, V. Gopalan, P. Kluth, Solid-state nanopore sensing reveals conformational changes induced by a mutation in a neuron-specific tRNAArg, Nucleic Acids Research, Volume 54, Issue 2, (2026), gkaf1411, doi: org/10.1093/nar/gkaf1411

  10. S. Saarinen, A. Sanz-Velasco, P. Indyka, M. Rawski, A. Biela, E. Anaya-Plaza, M. Kostiainen, Harnessing DNA Binding Proteins from Starved Cells for DNA Origami Protection, Small Structures, 7, 1, 2026, DOI: 10.1002/sstr.202500626

  11. D. Skoczek, D. Kloska, M. Targosz-Korecka, K. Szade, A.P. Biela, J. Hohendorff, M. Babincak, A. Kopacz, M.T. Malecki, J. Stepniewski, N. Kachamakova-Trojanowska, Integrated transcriptome and proteome analyses unveil cytoskeletal alterations in an endothelial model of monogenic diabetes, Genome Medicine, Volume 18,38 (2026), DOI: 10.1186/s13073-026-01615-z

2025

  1. A. D. Biela, T.-Y. Lin, M. Jaciuk, P. Indyka, M. Rawski, G. Ważny, A. Chramiec-Głąbik, D. Dobosz, B. Skupień-Rabian, U. Jankowska, J. Rappsilber, R. Schaffrath, S. Glatt, Determining the effects of pseudouridine incorporation on human tRNAs, The EMBO Journal, 44, 3553–3585 (2025) doi: 10.1038/s44318-025-00443-y.
  2. Ş. Ţălu, A. S. Cîmpean, M. A. Lungu, R. V. Ghita, L. Crăciun, F. Popescu, Effect of TiO₂ quantum dots incorporation on the nanoscale morphology and 3D spatial complexity of Photosystem II–enriched photosynthetic membranes, Surfaces and Interfaces, 72, 107076 (2025) doi: 10.1016/j.surfin.2025.107076.
  3. ​E. Esposito, F. Stanca, C. Carbone, L. F. Carafa, A. Puglisi, G. M. Musumeci, Nanovesicles and Human Skin Interaction: A Comparative Ex-Vivo Study, Nanomaterials, 15(12), 937 (2025) doi: 10.3390/nano15120937.
  4. G. Łazarski, M. Janion, W. Buczek, M. Brzozowski, P. Nowakowski, A. Jagieła, A. Osyczka, Interaction of Polystyrene Nanoplastic with Lipid Membranes, The Journal of Physical Chemistry B, 129(16), 4110–4122 (2025) doi: 10.1021/acs.jpcb.5c00738.
  5. M. E. Skalska, J. Oczkowska, M. Stępnik, K. Pawlak, E. Chmielewska, A. Górka, P. Kowalczyk, A. Wiktorska, T. Kowalczyk, ToF-SIMS revealing sphingolipids composition in extracellular vesicles and paternal β-cells after persistent hyperglycemia, Talanta, 297(A), 128582 (2025) doi: 10.1016/j.talanta.2025.128582.
  6. W. Guo, Y. Tang, H. Yang, M. Sheng, Y. Cheng, J. Sun, H. Zhang, J. Xu, Y. Chen, M. Gao, J. Chen, C. Yang, J. Wu, Y. Zhou, Queuosine is incorporated into precursor tRNA before splicing, Nature Communications, 16, 7044 (2025) doi: 10.1038/s41467-025-62220-z.
  7. S. Chamera, P. Grudnik, M. Siedlecki, M. Pawlik, K. Bąkowska-Żywicka, Structural and biochemical characterization of the 3′–5′ tRNA splicing ligases, Journal of Biological Chemistry, 301(5), 108506 (2025) doi: 10.1016/j.jbc.2025.108506.
  8. A. Silale, M. Madej, K. Mikruta, A. M. Frey, A. J. Hart, A. Baslé, C. Scavenius, J. J. Enghild, M. Trost, R. P. Hirt, B. van den Berg, Structure of a distinct β-barrel assembly machinery complex in the Bacteroidota, Nature Microbiology (2025) doi: 10.1038/s41564-025-02132-2.
  9. W. Guo, I. Kaczmarczyk, K. Kopietz, F. Flegler, S. Russo, E. Cigirgan, A. Chramiec-Głąbik, Ł. Koziej, C. Cirzi, J. Peschek, K. Reuter, M. Helm, S. Glatt, F. Tuorto, Queuosine is incorporated into precursor tRNA before splicing, Nature Communications, 16, 7044 (2025) doi: 10.1038/s41467-025-62220-z.

  10. N. Osinski, K. Majsterkiewicz, Z. Pakosz-Stepien, Y, Azuma, A.P. Biela, S. Gawel, J.G. Heddle, JG, Designed, Programmable Protein Cages Utilizing Diverse Metal Coordination Geometries Show Reversible, pH-Dependent Assembly, Macrmoleculer Rapid Communications, 46, 6, 2025, 2570018, DOI: 10.1002/marc.202400712

  11. A. Naskalska, M. Walczak, M. Bochenek, A. Dabrowska, A.P. Biela, J.G. Heddle, Cargo loading and surface display using enlarged MS2 virus-like particles, International Journal of Pharmaceutics, 125865, 682, 2025, DOI: 10.1016/j.ijpharm.2025.125865

  12. Abu-Baker, A. Al-Feghali, E. Zolfaghar, G. Velpula, A. Biela, S. De Feyter, J. Heddle, G. Cosa, A. Blum, Extended Plasmonic Nanostructures Templated by Tobacco Mosaic Virus Coat Protein, I. Small  21, 50, 7076, 2025, DOI: 10.1002/smll.202507076

  13. G. Bereta, E. Bielecka, K. Marzec, Ł. Pijanowski, A. Biela, P. Wilk, M. Kamińska, J. Nowak, E. Wątor-Wilk, P. Grudnik, D. Kowalczyk, J. Kozieł, P. Mydel, M. Poręba, T. Kantyka, Glycosaminoglycans activate peptidylarginine deiminase 4 by enhancing calcium affinity, Proceedings of the National Academy of Sciences of the United States of America, 122, 44, 508369122, 2025, DOI: 10.1073/pnas.2508369122 

2024

  1. S. Pintscher, R. Pietras, B. Mielecki, M. Szwalec, A. Wójcik-Augustyn, P. Indyka, M. Rawski, Ł. Koziej, M. Jaciuk, G. Ważny, S. Glatt, A. Osyczka, J. Alric, Molecular basis of plastoquinone reduction in plant cytochrome b6f, Nature Plants, 10(11), 1814–1825 (2024) doi: 10.1038/s41477-024-01804-x.
  2. N.-E.-H. Abbassi, M. Jaciuk, D. Scherf, P. Böhnert, A. Rau, A. Hammermeister, M. Rawski, P. Indyka, G. Ważny, A. Chramiec-Głąbik, D. Dobosz, B. Skupien-Rabian, U. Jankowska, J. Rappsilber, R. Schaffrath, T.-Y. Lin, S. Glatt, Cryo-EM structures of the human Elongator complex at work, Nature Communications, 15, 4094 (2024) doi: 10.1038/s41467-024-48251-y.
  3. T.-Y. Lin, L. Kleemann, J. Jeżowski, D. Dobosz, M. Rawski, P. Indyka, G. Ważny, R. Mehta, A. Chramiec-Głąbik, Ł. Koziej, T. Ranff, S. Glatt, The molecular basis of tRNA selectivity by human pseudouridine synthase 3, Molecular Cell, 84(13), 2472–2489.e8 (2024) doi: 10.1016/j.molcel.2024.06.013.
  4. N. G. Badepally, T. R. de Moura, E. Purta, E. F. Baulin, J. M. Bujnicki, Cryo-EM structure of raiA ncRNA from Clostridium reveals a new RNA 3D fold, Journal of Molecular Biology, 436(23), 168833 (2024) doi: 10.1016/j.jmb.2024.168833.
  5. E. Michalczyk, M. Janion, P. Nowakowski, M. Brzozowski, A. Jagieła, A. Mielczarek, W. Buczek, A. Osyczka, Structural basis of chiral wrap and T-segment capture by Escherichia coli DNA gyrase, PNAS, 121(49), e2407398121 (2024) doi: 10.1073/pnas.2407398121.
  6. M. Sokołowski, D. Kwaśna, K. E. Ravichandran, C. Eggers, R. Krutyhołowa, M. Kaczmarczyk, B. Skupień-Rabian, M. Jaciuk, M. Walczak, P. Dahate, M. Pabiś, M. Jemioła-Rzemińska, U. Jankowska, S. A. Leidel, S. Glatt, Molecular basis for thiocarboxylation and release of Urm1 by its E1-activating enzyme Uba4, Nucleic Acids Research, 52(22), 13980–13995 (2024) doi: 10.1093/nar/gkae1111.
  7. K. Mikruta, M. Madej, A Factory of Bacterial Weaponry, Academia. The Magazine of the Polish Academy of Sciences, 4(84), 44–47 (2024) doi: 10.24425/academiaPAS.2024.152930.
  8. N. Osiński, K. Majsterkiewicz, Z. Pakosz-Stępień, Y. Azuma, A. P. Biela, S. Gaweł, J. G. Heddle, Designed, Programmable Protein Cages Utilizing Diverse Metal Coordination Geometries Show Reversible, pH-Dependent Assembly, Macromolecular Rapid Communications, 46(6), e2400712 (2025; e-pub 2024) doi: 10.1002/marc.202400712.
  9. E. Wątor, P. Wilk, P. Kochanowski, P. Grudnik, Structural characterization of the (deoxy)hypusination in Trichomonas vaginalis questions the bifunctionality of deoxyhypusine synthase, The FEBS Journal, 291(17), 3856–3869 (2024) doi: 10.1111/febs.17207.
  10.  A. Matsuda, A. Li, A. Tsuchiya, A. Nishimura, M. Onodera, M. J. Shieh, S. Kikkawa, S. Imami, T. Yoshizawa, Y. Suzuki, Despite the odds: formation of the SARS-CoV-2 methylation complex, Nucleic Acids Research, 52(11), 6441–6458 (2024) doi: 10.1093/nar/gkae165.
  11. W. Witek, M. Waligórska, A. A. Śliwiak, M. Gaweł, E. Janion, M. Nowakowska, P. Stępień, A. Osyczka, Targeting imidazole-glycerol phosphate dehydratase in plants: novel approach for structural and functional studies, and inhibitor blueprinting, Frontiers in Plant Science, 15, 1343980 (2024) doi: 10.3389/fpls.2024.1343980.
  12. S. Chamera, M. Siedlecki, K. Bąkowska-Żywicka, P. Grudnik, P. Wysocki, Cryo-EM structure of rotavirus B NSP2 reveals its unique tertiary structure and RNA binding mode, Journal of Virology, 98(3), e01660-23 (2024) doi: 10.1128/jvi.01660-23.
  13.  T. R. de Moura, E. Purta, N. G. Badepally, E. F. Baulin, J. M. Bujnicki, Conserved structures and dynamics in 5′-proximal regions of Betacoronavirus RNA genomes, Nucleic Acids Research, 52(6), 3419–3432 (2024) doi: 10.1093/nar/gkae144.

2023

  1. P. Stępień, M. Bester, R. Sacharczuk, M. Pawlik, A. Madej, Ł. Koziej, M. Rawski, P. Indyka, G. Ważny, J. Jasiński, S. Glatt, A. Osyczka, CRAFTing Delivery of Membrane Proteins into Protocells using Nanodiscs, ACS Applied Materials & Interfaces, 15(49), 56689–56701 (2023) doi: 10.1021/acsami.3c11894.

2021

  1. M. Nowacka, E. Nowak, M. Czarnocki-Cieciura, J. Jackiewicz, K. Skowronek, R. H. Szczepanowski, B. M. Wöhrl, M. Nowotny, Structures of Substrate Complexes of Foamy Viral Protease-Reverse Transcriptase, Journal of Virology, 95(18), e00848-21 (2021) doi: 10.1128/JVI.00848-21.