| 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 |
| 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 |
| 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 |
| Dynamics and mechanism of a light-driven chloride pump
Mous, S., Gotthard, G., Ehrenberg, D., Sen, S., Weinert, T., Johnson, P. J. M., … Nogly, P. (2022). Dynamics and mechanism of a light-driven chloride pump. Science, 375(6583), 845-851. https://doi.org/10.1126/science.abj6663 |
| 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 |
| Iterative structure-based optimization of short peptides targeting the bacterial sliding clamp
Monsarrat, C., Compain, G., André, C., Engilberge, S., Martiel, I., Oliéric, V., … Burnouf, D. Y. (2021). Iterative structure-based optimization of short peptides targeting the bacterial sliding clamp. Journal of Medicinal Chemistry, 64(23), 17063-17078. https://doi.org/10.1021/acs.jmedchem.1c00918 |
| Pink-beam serial femtosecond crystallography for accurate structure-factor determination at an X-ray free-electron laser
Nass, K., Bacellar, C., Cirelli, C., Dworkowski, F., Gevorkov, Y., James, D., … Milne, C. J. (2021). Pink-beam serial femtosecond crystallography for accurate structure-factor determination at an X-ray free-electron laser. IUCrJ, 8, 905-920. https://doi.org/10.1107/S2052252521008046 |
| Fabrication of ultrathin suspended polymer membranes as supports for serial protein crystallography
Karpik, A., Martiel, I., Kristiansen, P. M., & Padeste, C. (2020). Fabrication of ultrathin suspended polymer membranes as supports for serial protein crystallography. Micro and Nano Engineering, 7, 100053 (6 pp.). https://doi.org/10.1016/j.mne.2020.100053 |
| 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 |
| The TELL automatic sample changer for macromolecular crystallography
Martiel, I., Buntschu, D., Meier, N., Gobbo, A., Panepucci, E., Schneider, R., … Wang, M. (2020). The TELL automatic sample changer for macromolecular crystallography. Journal of Synchrotron Radiation, 27, 860-863. https://doi.org/10.1107/S1600577520002416 |
| X-ray fluorescence detection for serial macromolecular crystallography using a JUNGFRAU pixel detector
Martiel, I., Mozzanica, A., Opara, N. L., Panepucci, E., Leonarski, F., Redford, S., … Wang, M. (2020). X-ray fluorescence detection for serial macromolecular crystallography using a JUNGFRAU pixel detector. Journal of Synchrotron Radiation, 27, 329-339. https://doi.org/10.1107/S1600577519016758 |
| 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 |
| A compact and cost-effective hard X-ray free-electron laser driven by a high-brightness and low-energy electron beam
Prat, E., Abela, R., Aiba, M., Alarcon, A., Alex, J., Arbelo, Y., … Zimoch, E. (2020). A compact and cost-effective hard X-ray free-electron laser driven by a high-brightness and low-energy electron beam. Nature Photonics, 14, 748-754. https://doi.org/10.1038/s41566-020-00712-8 |
| 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 |
| Interaction of a model peptide on gram negative and gram positive bacterial sliding clamps
André, C., Martiel, I., Wolff, P., Landolfo, M., Lorber, B., Silva da Veiga, C., … Burnouf, D. Y. (2019). Interaction of a model peptide on gram negative and gram positive bacterial sliding clamps. ACS Infectious Diseases, 5, 1022-1034. https://doi.org/10.1021/acsinfecdis.9b00089 |
| Strategies for sample delivery for femtosecond crystallography
Martiel, I., Müller-Werkmeister, H. M., & Cohen, A. E. (2019). Strategies for sample delivery for femtosecond crystallography. Acta Crystallographica Section D: Structural Biology, 75(2), 160-177. https://doi.org/10.1107/S2059798318017953 |
| Practical approaches for in situ X-ray crystallography: from high-throughput screening to serial data collection
Martiel, I., Olieric, V., Caffrey, M., & Wang, M. (2018). Practical approaches for in situ X-ray crystallography: from high-throughput screening to serial data collection. In K. Beis & G. Evans (Eds.), Chemical biology: Vol. 8. Protein crystallography: challenges and practical solutions (pp. 1-27). https://doi.org/10.1039/9781788010504-00001 |
| Design of ultra-swollen lipidic mesophases for the crystallization of membrane proteins with large extracellular domains
Zabara, A., Chong, J. T. Y., Martiel, I., Stark, L., Cromer, B. A., Speziale, C., … Mezzenga, R. (2018). Design of ultra-swollen lipidic mesophases for the crystallization of membrane proteins with large extracellular domains. Nature Communications, 9(1), 544. https://doi.org/10.1038/s41467-018-02996-5 |
| SwissFEL: the Swiss X-ray free electron laser
Milne, C. J., Schietinger, T., Aiba, M., Alarcon, A., Alex, J., Anghel, A., … Braun, H. H. (2017). SwissFEL: the Swiss X-ray free electron laser. Applied Sciences, 7(7), 720 (57 pp.). https://doi.org/10.3390/app7070720 |
| Direct protein crystallization on ultrathin membranes for diffraction measurements at X-ray free-electron lasers
Opara, N., Martiel, I., Arnold, S. A., Braun, T., Stahlberg, H., Makita, M., … Padeste, C. (2017). Direct protein crystallization on ultrathin membranes for diffraction measurements at X-ray free-electron lasers. Journal of Applied Crystallography, 50(3), 909-918. https://doi.org/10.1107/S1600576717005799 |
