Publications using BECM data

Torino, S., Dhurandhar, M., Stroobants, A., et al.; Time-resolved cryo-EM using a combination of droplet microfluidics with on-demand jetting, Nat Methods. 2023 Sep;20(9):1400-1408. doi: 10.1038/s41592-023-01967-z, https://www.nature.com/articles/s41592-023-01967-z

De Gieter, S., Gallagher, C.I., Wijckmans, E., et al.; Sterol derivative binding to the orthosteric site causes conformational changes in an invertebrate Cys-loop receptor, Elife. 2023 Jul 3;12:e86029. doi: 10.7554/eLife.86029, https://elifesciences.org/articles/86029

Fernandez, M., Shkumatov, A.V., Liu, Y., et al.; AFM-based force spectroscopy unravels stepwise formation of the DNA transposition complex in the widespread Tn3 family mobile genetic elements, Nucleic Acids Res. 2023 Jun 9;51(10):4929-4941. doi: 10.1093/nar/gkad241, https://academic.oup.com/nar/article/51/10/4929/7110757

Claridge, J.K., Martens, C., Pradhan, B., et al.; The folding-limited nucleation of curli hints at an evolved safety mechanism for functional amyloid production, bioRxiv, 2023.05. 26.542396, https://www.biorxiv.org/content/10.1101/2023.05.26.542396v1

Sleutel, M., Pradhan, B., Volkov, A.N., Remaut, H.; Structural analysis and architectural principles of the bacterial amyloid curli, Nature Communications 14 (1), 2822, https://www.nature.com/articles/s41467-023-38204-2

Tsirigotaki, A., Dansercoer, A., Verschueren, K.H.G., et al.; Mechanism of receptor assembly via the pleiotropic adipokine Leptin, Nature Structural & Molecular Biology 30 (4), 551-563, https://www.nature.com/articles/s41594-023-00941-9

Bloch, Y., Felix, J., Merceron, R., et al.; Structures of complete extracellular receptor assemblies mediated by IL-12 and IL-23, (2023) bioRxiv, 2023.03.13.532366, https://www.biorxiv.org/content/10.1101/2023.03.13.532366v1 (accepted at Nature Structural & Molecular Biology)

Dupuy, E., Van der Verren, S.E., Lin, J. et al.; A molecular device for the redox quality control of GroEL/ES substrates, Cell 186 (5), 1039-1049. e17, https://www.sciencedirect.com/science/article/pii/S0092867423000430

Fioravanti, A., Mathelie-Guinlet, M., Dufrêne, Y.F., Remaut, H.; The Bacillus anthracis S-layer is an exoskeleton-like structure that imparts mechanical and osmotic stabilization to the cell wall, PNAS nexus 1 (4), September 2022,  pgac121, https://academic.oup.com/pnasnexus/article/1/4/pgac121/6655932

Shkumatov, A.V., Aryanpour, N., Oger, C.A., et al.; Structural insight into Tn3 family transposition mechanism,  Nature Communications,  13, Article number: 6155 (2022), https://www.nature.com/articles/s41467-022-33871-z

Kolata, P. & Efremov, R.G.; Structure of Escherichia coli respiratory complex I reconstituted into lipid nanodiscs reveals an uncoupled conformation,  eLife 2021;10:e68710 DOI: 10.7554/eLife.68710

Pradhan, B., Liedtke, J. Sleutel, M., et al; Endospore Appendages: a novel pilus superfamily from the endospores of pathogenic Bacilli, EMBO J 2021:e106887 https://doi.org/10.15252/embj.2020106887

Efremov, R.G. & Stroobants, A.; Coma-corrected rapid single-particle cryo-EM data collection on the CRYO ARM 300, Acta Cryst. 2021, D77, 555-564
https://doi.org/10.1107/S2059798321002151

Fislage, M., Shkumatov, A.V., Stroobants, A. & Efremov, R.G.; Assessing the JEOL CRYO ARM 300 for high-throughput automated single-particle cryo-EM in a multiuser environment; IUCrJ, Volume 7, Part 4, 2020, pp. 707-718,https://doi.org/10.1107/S2052252520006065