| 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 |
| Crystal structures of human and mouse ketohexokinase provide a structural basis for species- and isoform-selective inhibitor design
Ebenhoch, R., Bauer, M., Romig, H., Gottschling, D., Kley, J. T., Heine, N., … Pautsch, A. (2023). Crystal structures of human and mouse ketohexokinase provide a structural basis for species- and isoform-selective inhibitor design. Acta Crystallographica Section D: Structural Biology, 79(10), 871-880. https://doi.org/10.1107/S2059798323006137 |
| Structure of reverse gyrase with a minimal latch that supports ATP-dependent positive supercoiling without specific interactions with the topoisomerase domain
Mhaindarkar, V. P., Rasche, R., Kümmel, D., Rudolph, M. G., & Klostermeier, D. (2023). Structure of reverse gyrase with a minimal latch that supports ATP-dependent positive supercoiling without specific interactions with the topoisomerase domain. Acta Crystallographica Section D: Structural Biology, 79(6), 498-507. https://doi.org/10.1107/S2059798323002565 |
| Structural insight into an anti-BRIL Fab as a G-protein-coupled receptor crystallization chaperone
Miyagi, H., Suzuki, M., Yasunaga, M., Asada, H., Iwata, S., & Saito, Jichi. (2023). Structural insight into an anti-BRIL Fab as a G-protein-coupled receptor crystallization chaperone. Acta Crystallographica Section D: Structural Biology, 79(5), 435-441. https://doi.org/10.1107/S205979832300311X |
| 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 |
| Correction of rhodopsin serial crystallography diffraction intensities for a lattice-translocation defect
Rodrigues, M. J., Casadei, C. M., Weinert, T., Panneels, V., & Schertler, G. F. X. (2023). Correction of rhodopsin serial crystallography diffraction intensities for a lattice-translocation defect. Acta Crystallographica Section D: Structural Biology, 79(3), D79 (10 pp.). https://doi.org/10.1107/S2059798323000931 |
| Atypical homodimerization revealed by the structure of the <em>(S)</em>-enantioselective haloalkane dehalogenase DmmarA from <em>Mycobacterium marinum</em>
Snajdarova, K., Marques, S. M., Damborsky, J., Bednar, D., & Marek, M. (2023). Atypical homodimerization revealed by the structure of the (S)-enantioselective haloalkane dehalogenase DmmarA from Mycobacterium marinum. Acta Crystallographica Section D: Structural Biology, 79(Pt 11), 956-970. https://doi.org/10.1107/S2059798323006642 |
| Lipidic cubic phase serial femtosecond crystallography structure of a photosynthetic reaction centre
Båth, P., Banacore, A., Börjesson, P., Bosman, R., Wickstrand, C., Safari, C., … Neutze, R. (2022). Lipidic cubic phase serial femtosecond crystallography structure of a photosynthetic reaction centre. Acta Crystallographica Section D: Structural Biology, 78(6), 698-708. https://doi.org/10.1107/S2059798322004144 |
| A scalable strategy to solve structures of PDZ domains and their complexes
Cousido-Siah, A., Carneiro, L., Kostmann, C., Ecsedi, P., Nyitray, L., Trave, G., & Gogl, G. (2022). A scalable strategy to solve structures of PDZ domains and their complexes. Acta Crystallographica Section D: Structural Biology, 78, 509-516. https://doi.org/10.1107/S2059798322001784 |
| High-resolution structures of the bound effectors avadomide (CC-122) and iberdomide (CC-220) highlight advantages and limitations of the MsCI4 soaking system
Heim, C., & Hartmann, M. D. (2022). High-resolution structures of the bound effectors avadomide (CC-122) and iberdomide (CC-220) highlight advantages and limitations of the MsCI4 soaking system. Acta Crystallographica Section D: Structural Biology, 78, 290-298. https://doi.org/10.1107/S2059798322000092 |
| 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 |
| Structure of a hydrophobic leucinostatin derivative determined by host lattice display
Kiss, C., Gall, F. M., Dreier, B., Adams, M., Riedl, R., Plückthun, A., & Mittl, P. R. E. (2022). Structure of a hydrophobic leucinostatin derivative determined by host lattice display. Acta Crystallographica Section D: Structural Biology, 78(12), 1439-1450. https://doi.org/10.1107/S2059798322010762 |
| Statistically correcting dynamical electron scattering improves the refinement of protein nanocrystals, including charge refinement of coordinated metals
Blum, T. B., Housset, D., Clabbers, M. T. B., van Genderen, E., Bacia-Verloop, M., Zander, U., … Abrahams, J. P. (2021). Statistically correcting dynamical electron scattering improves the refinement of protein nanocrystals, including charge refinement of coordinated metals. Acta Crystallographica Section D: Structural Biology, 77, 75-85. https://doi.org/10.1107/S2059798320014540 |
| <em>IceBear</em>: an intuitive and versatile web application for research-data tracking from crystallization experiment to PDB deposition
Daniel, E., Maksimainen, M. M., Smith, N., Ratas, V., Biterova, E., Murthy, S. N., … Wierenga, R. K. (2021). IceBear: an intuitive and versatile web application for research-data tracking from crystallization experiment to PDB deposition. Acta Crystallographica Section D: Structural Biology, 77, 151-163. https://doi.org/10.1107/S2059798320015223 |
| 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 |
| Making a difference in multi-data-set crystallography: simple and deterministic data-scaling/selection methods
Assmann, G. M., Wang, M., & Diederichs, K. (2020). Making a difference in multi-data-set crystallography: simple and deterministic data-scaling/selection methods. Acta Crystallographica Section D: Structural Biology, 76, 636-652. https://doi.org/10.1107/S2059798320006348 |
| Macromolecular X-ray crystallography: soon to be a road less travelled?
Beale, J. H. (2020). Macromolecular X-ray crystallography: soon to be a road less travelled? Acta Crystallographica Section D: Structural Biology, 76(5), 400-405. https://doi.org/10.1107/S2059798320004660 |
| Exploring the complex map of insulin polymorphism: a novel crystalline form in the presence of <em>m</em>-cresol
Karavassili, F., Valmas, A., Dimarogona, M., Giannopoulou, A. E., Fili, S., Norrman, M., … Margiolaki, I. (2020). Exploring the complex map of insulin polymorphism: a novel crystalline form in the presence of m-cresol. Acta Crystallographica Section D: Structural Biology, 76, 366-374. https://doi.org/10.1107/S2059798320002545 |
| The copper(II)-binding tripeptide GHK, a valuable crystallization and phasing tag for macromolecular crystallography
Mehr, A., Henneberg, F., Chari, A., Görlich, D., & Huyton, T. (2020). The copper(II)-binding tripeptide GHK, a valuable crystallization and phasing tag for macromolecular crystallography. Acta Crystallographica Section D: Structural Biology, 76(12), 1222-1232. https://doi.org/10.1107/S2059798320013741 |