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Peptide-based covalent inhibitors bearing mild electrophiles to target a conserved his residue of the bacterial sliding clamp
Compain, G., Monsarrat, C., Blagojevic, J., Brillet, K., Dumas, P., Hammann, P., … Guichard, G. (2024). Peptide-based covalent inhibitors bearing mild electrophiles to target a conserved his residue of the bacterial sliding clamp. JACS Au, 4(2), 432-440. https://doi.org/10.1021/jacsau.3c00572
Light-oxygen-voltage (LOV)-sensing domains: activation mechanism and optogenetic stimulation
Flores-Ibarra, A., Maia, R. N. A., Olasz, B., Church, J. R., Gotthard, G., Schapiro, I., … Nogly, P. (2024). Light-oxygen-voltage (LOV)-sensing domains: activation mechanism and optogenetic stimulation. Journal of Molecular Biology, 436(5), 168356 (19 pp.). https://doi.org/10.1016/j.jmb.2023.168356
Fragment-based screening targeting an open form of the SARS-CoV-2 main protease binding pocket
Huang, C. Y., Metz, A., Lange, R., Artico, N., Potot, C., Hazemann, J., … Mac Sweeney, A. (2024). Fragment-based screening targeting an open form of the SARS-CoV-2 main protease binding pocket. Acta Crystallographica Section D: Structural Biology, 80, 123-136. https://doi.org/10.1107/S2059798324000329
RNA oligomers at atomic resolution containing 1-methylpseudouridine, an essential building block of mRNA vaccines
Nievergelt, P., Berliat, F., McAuley, K. E., Dorgan, C. R., van Well, R. M., Thorn, A., & Spingler, B. (2024). RNA oligomers at atomic resolution containing 1-methylpseudouridine, an essential building block of mRNA vaccines. ChemMedChem. https://doi.org/10.1002/cmdc.202300600
Se-MAG is a convenient additive for experimental phasing and structure determination of membrane proteins crystallised by the lipid cubic phase (in meso) method
Boland, C., Huang, C. Y., Shanker Kaki, S., Wang, M., Olieric, V., & Caffrey, M. (2023). Se-MAG is a convenient additive for experimental phasing and structure determination of membrane proteins crystallised by the lipid cubic phase (in meso) method. Crystals, 13(9), 1402 (20 pp.). https://doi.org/10.3390/cryst13091402
Micro-structured polymer fixed targets for serial crystallography at synchrotrons and XFELs
Carrillo, M., Mason, T. J., Karpik, A., Martiel, I., Kepa, M. W., McAuley, K. E., … Padeste, C. (2023). Micro-structured polymer fixed targets for serial crystallography at synchrotrons and XFELs. IUCrJ, 10(6), 678-693. https://doi.org/10.1107/S2052252523007595
Time-resolved crystallography captures light-driven DNA repair
Christou, N. E., Apostolopoulou, V., Melo, D. V. M., Ruppert, M., Fadini, A., Henkel, A., … Lane, T. J. (2023). Time-resolved crystallography captures light-driven DNA repair. Science, 382(6674), 1015-1020. https://doi.org/10.1126/science.adj4270
Ultrafast structural changes direct the first molecular events of vision
Gruhl, T., Weinert, T., Rodrigues, M. J., Milne, C. J., Ortolani, G., Nass, K., … Panneels, V. (2023). Ultrafast structural changes direct the first molecular events of vision. Nature, 615, 939-944. https://doi.org/10.1038/s41586-023-05863-6
A standard descriptor for fixed-target serial crystallography
Owen, R. L., de Sanctis, D., Pearson, A. R., & Beale, J. H. (2023). A standard descriptor for fixed-target serial crystallography. Acta Crystallographica Section D: Structural Biology, 79(8), 668-672. https://doi.org/10.1107/S2059798323005429
Identification of the SARS-unique domain of SARS-CoV-2 as an antiviral target
Qin, B., Li, Z., Tang, K., Wang, T., Xie, Y., Aumonier, S., … Cui, S. (2023). Identification of the SARS-unique domain of SARS-CoV-2 as an antiviral target. Nature Communications, 14(1), 3999 (13 pp.). https://doi.org/10.1038/s41467-023-39709-6
SDU - software for high-throughput automated data collection at the Swiss Light Source
Smith, K. M. L., Panepucci, E., Kaminski, J. W., Aumonier, S., Huang, C. Y., Eris, D., … Wojdyla, J. A. (2023). SDU - software for high-throughput automated data collection at the Swiss Light Source. Journal of Synchrotron Radiation, 30, 538-545. https://doi.org/10.1107/S1600577523002631
Structure snapshots reveal the mechanism of a bacterial membrane lipoprotein <em>N</em>-acyltransferase
Smithers, L., Degtjarik, O., Weichert, D., Huang, C. Y., Boland, C., Bowen, K., … Caffrey, M. (2023). Structure snapshots reveal the mechanism of a bacterial membrane lipoprotein N-acyltransferase. Science Advances, 9(26), eadf5799 (17 pp.). https://doi.org/10.1126/sciadv.adf5799
A multi-reservoir extruder for time-resolved serial protein crystallography and compound screening at X-ray free-electron lasers
Wranik, M., Kepa, M. W., Beale, E. V., James, D., Bertrand, Q., Weinert, T., … Standfuss, J. (2023). A multi-reservoir extruder for time-resolved serial protein crystallography and compound screening at X-ray free-electron lasers. Nature Communications, 14(1), 7956 (12 pp.). https://doi.org/10.1038/s41467-023-43523-5
Watching the release of a photopharmacological drug from tubulin using time-resolved serial crystallography
Wranik, M., Weinert, T., Slavov, C., Masini, T., Furrer, A., Gaillard, N., … Standfuss, J. (2023). Watching the release of a photopharmacological drug from tubulin using time-resolved serial crystallography. Nature Communications, 14(1), 903 (12 pp.). https://doi.org/10.1038/s41467-023-36481-5
Filling of a water-free void explains the allosteric regulation of the β<sub>1</sub>-adrenergic receptor by cholesterol
Abiko, L. A., Dias Teixeira, R., Engilberge, S., Grahl, A., Mühlethaler, T., Sharpe, T., & Grzesiek, S. (2022). Filling of a water-free void explains the allosteric regulation of the β1-adrenergic receptor by cholesterol. Nature Chemistry, 14, 1133-1141. https://doi.org/10.1038/s41557-022-01009-9
Biochemical, structural, and functional studies reveal that MAB_4324c from <em>Mycobacterium abscessus</em> is an active tandem repeat <em>N</em>‐acetyltransferase
Alsarraf, H. M. A. B., Ung, K. L., Johansen, M. D., Dimon, J., Olieric, V., Kremer, L., & Blaise, M. (2022). Biochemical, structural, and functional studies reveal that MAB_4324c from Mycobacterium abscessus is an active tandem repeat N‐acetyltransferase. FEBS Letters, 596(12), 1516-1532. https://doi.org/10.1002/1873-3468.14360
Slow protein dynamics probed by time-resolved oscillation crystallography at room temperature
Aumonier, S., Engilberge, S., Caramello, N., von Stetten, D., Gotthard, G., Leonard, G. A., … Royant, A. (2022). Slow protein dynamics probed by time-resolved oscillation crystallography at room temperature. IUCrJ, 9(6), 756-767. https://doi.org/10.1107/S2052252522009150
Structure–function relationship of a novel fucoside-binding fruiting body lectin from <em>Coprinopsis cinerea</em> exhibiting nematotoxic activity
Bleuler-Martinez, S., Varrot, A., Olieric, V., Schubert, M., Vogt, E., Fetz, C., … Künzler, M. (2022). Structure–function relationship of a novel fucoside-binding fruiting body lectin from Coprinopsis cinerea exhibiting nematotoxic activity. Glycobiology, 32(7), 600-615. https://doi.org/10.1093/glycob/cwac020
Structural basis of the radical pair state in photolyases and cryptochromes
Cellini, A., Shankar, M. K., Wahlgren, W. Y., Nimmrich, A., Furrer, A., James, D., … Westenhoff, S. (2022). Structural basis of the radical pair state in photolyases and cryptochromes. Chemical Communications, 58(31), 4889-4892. https://doi.org/10.1039/D2CC00376G
Chimeric single α-helical domains as rigid fusion protein connections for protein nanotechnology and structural biology
Collu, G., Bierig, T., Krebs, A. S., Engilberge, S., Varma, N., Guixà-González, R., … Benoit, R. M. (2022). Chimeric single α-helical domains as rigid fusion protein connections for protein nanotechnology and structural biology. Structure, 30(1), 95-106. https://doi.org/10.1016/j.str.2021.09.002
 

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