| 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 |
| Probing ligand binding of endothiapepsin by 'temperature-resolved' macromolecular crystallography
Huang, C. Y., Aumonier, S., Engilberge, S., Eris, D., Smith, K. M. L., Leonarski, F., … Wang, M. (2022). Probing ligand binding of endothiapepsin by 'temperature-resolved' macromolecular crystallography. Acta Crystallographica Section D: Structural Biology, 78, 964-974. https://doi.org/10.1107/S205979832200612X |
| Fast fragment- and compound-screening pipeline at the Swiss Light Source
Kaminski, J. W., Vera, L., Stegmann, D. P., Vering, J., Eris, D., Smith, K. M. L., … Sharpe, M. E. (2022). Fast fragment- and compound-screening pipeline at the Swiss Light Source. Acta Crystallographica Section D: Structural Biology, 78, 328-336. https://doi.org/10.1107/S2059798322000705 |
| Elucidation of a nutlin-derivative-HDM2 complex structure at the interaction site by NMR molecular replacement: a straightforward derivation
Mertens, V., Abi Saad, M. J., Coudevylle, N., Wälti, M. A., Finke, A., Marsh, M., & Orts, J. (2022). Elucidation of a nutlin-derivative-HDM2 complex structure at the interaction site by NMR molecular replacement: a straightforward derivation. Journal of Magnetic Resonance Open, 10-11, 100032 (5 pp.). https://doi.org/10.1016/j.jmro.2022.100032 |
| Crystal structure of the pheromone E<em>r</em>-13 from the ciliate <em>Euplotes raikovi</em>, with implications for a protein-protein association model in pheromone/receptor interactions
Pedrini, B., Finke, A. D., Marsh, M., Luporini, P., Vallesi, A., & Alimenti, C. (2022). Crystal structure of the pheromone Er-13 from the ciliate Euplotes raikovi, with implications for a protein-protein association model in pheromone/receptor interactions. Journal of Structural Biology, 214(1), 107812 (10 pp.). https://doi.org/10.1016/j.jsb.2021.107812 |
| Optimizing the growth of endothiapepsin crystals for serial crystallography experiments
Beale, J. H., & Marsh, M. E. (2021). Optimizing the growth of endothiapepsin crystals for serial crystallography experiments. Journal of Visualized Experiments, 168, e61896 (30 pp.). https://doi.org/10.3791/61896 |
| Crystal structure of the catalytic domain of botulinum neurotoxin subtype A3
Leka, O., Wu, Y., Li, X., & Kammerer, R. A. (2021). Crystal structure of the catalytic domain of botulinum neurotoxin subtype A3. Journal of Biological Chemistry, 296, 100684 (8 pp.). https://doi.org/10.1016/j.jbc.2021.100684 |
| Versatile microporous polymer-based supports for serial macromolecular crystallography
Martiel, I., Beale, J. H., Karpik, A., Huang, C. Y., Vera, L., Olieric, N., … Padeste, C. (2021). Versatile microporous polymer-based supports for serial macromolecular crystallography. Acta Crystallographica Section D: Structural Biology, 77(9), 1153-1167. https://doi.org/10.1107/S2059798321007324 |
| Comprehensive analysis of binding sites in tubulin
Mühlethaler, T., Gioia, D., Prota, A. E., Sharpe, M. E., Cavalli, A., & Steinmetz, M. O. (2021). Comprehensive analysis of binding sites in tubulin. Angewandte Chemie International Edition, 60(24), 13331-13342. https://doi.org/10.1002/anie.202100273 |
| Fragment-screening and automation at the Swiss Light Source macromolecular crystallography beamlines
Sharpe, M. E., & Wojdyla, J. A. (2021). Fragment-screening and automation at the Swiss Light Source macromolecular crystallography beamlines. Nihon Kessho Gakkaishi, 63(3), 232-235. https://doi.org/10.5940/jcrsj.63.232 |
| Combining high-throughput synthesis and high-throughput protein crystallography for accelerated hit identification
Sutanto, F., Shaabani, S., Oerlemans, R., Eris, D., Patil, P., Hadian, M., … Dömling, A. (2021). Combining high-throughput synthesis and high-throughput protein crystallography for accelerated hit identification. Angewandte Chemie International Edition, 60(33), 18231-18239. https://doi.org/10.1002/anie.202105584 |
| Selectively disrupting m<sup>6</sup>A-dependent protein-RNA interactions with fragments
Bedi, R. K., Huang, D., Wiedmer, L., Li, Y., Dolbois, A., Wojdyla, J. A., … Sledz, P. (2020). Selectively disrupting m6A-dependent protein-RNA interactions with fragments. ACS Chemical Biology, 15(3), 618-625. https://doi.org/10.1021/acschembio.9b00894 |
| <em>In situ</em> crystallography as an emerging method for structure solution of membrane proteins: the case of CCR2A
Cheng, R., Huang, C. Y., Hennig, M., Nar, H., & Schnapp, G. (2020). In situ crystallography as an emerging method for structure solution of membrane proteins: the case of CCR2A. FEBS Journal, 287(5), 866-873. https://doi.org/10.1111/febs.15098 |
| Structural refinement of the tubulin ligand (+)-discodermolide to attenuate chemotherapy-mediated senescence
Guo, B., Rodriguez-Gabin, A., Prota, A. E., Mühlethaler, T., Zhang, N., Ye, K., … McDaid, H. M. (2020). Structural refinement of the tubulin ligand (+)-discodermolide to attenuate chemotherapy-mediated senescence. Molecular Pharmacology, 98(2), 156-167. https://doi.org/10.1124/mol.119.117457 |
| 3D-printed holders for <em>in meso in situ</em> fixed-target serial X-ray crystallography
Huang, C. Y., Meier, N., Caffrey, M., Wang, M., & Olieric, V. (2020). 3D-printed holders for in meso in situ fixed-target serial X-ray crystallography. Journal of Applied Crystallography, 53, 854-859. https://doi.org/10.1107/S1600576720002897 |
| Low-dose <em>in situ</em> prelocation of protein microcrystals by 2D X-ray phase-contrast imaging for serial crystallography
Martiel, I., Huang, C. Y., Villanueva-Perez, P., Panepucci, E., Basu, S., Caffrey, M., … Wang, M. (2020). Low-dose in situ prelocation of protein microcrystals by 2D X-ray phase-contrast imaging for serial crystallography. IUCrJ, 7(6), 1131-1141. https://doi.org/10.1107/S2052252520013238 |
| Advances in long-wavelength native phasing at X-ray free-electron lasers
Nass, K., Cheng, R., Vera, L., Mozzanica, A., Redford, S., Ozerov, D., … Milne, C. J. (2020). Advances in long-wavelength native phasing at X-ray free-electron lasers. IUCrJ, 7, 965-975. https://doi.org/10.1107/S2052252520011379 |
| Femtosecond-to-millisecond structural changes in a light-driven sodium pump
Skopintsev, P., Ehrenberg, D., Weinert, T., James, D., Kar, R. K., Johnson, P. J. M., … Standfuss, J. (2020). Femtosecond-to-millisecond structural changes in a light-driven sodium pump. Nature, 583, 314-318. https://doi.org/10.1038/s41586-020-2307-8 |
| Crystal structure of CC chemokine receptor 2A in complex with an orthosteric antagonist provides insights for the design of selective antagonists
Apel, A. K., Cheng, R. K. Y., Tautermann, C. S., Brauchle, M., Huang, C. Y., Pautsch, A., … Schnapp, G. (2019). Crystal structure of CC chemokine receptor 2A in complex with an orthosteric antagonist provides insights for the design of selective antagonists. Structure, 27(3), 427-438.e5. https://doi.org/10.1016/j.str.2018.10.027 |
| Automated data collection and real-time data analysis suite for serial synchrotron crystallography
Basu, S., Kaminski, J. W., Panepucci, E., Huang, C. Y., Warshamanage, R., Wang, M., & Wojdyla, J. A. (2019). Automated data collection and real-time data analysis suite for serial synchrotron crystallography. Journal of Synchrotron Radiation, 26(1), 244-252. https://doi.org/10.1107/S1600577518016570 |
