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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
&lt;em&gt;IceBear&lt;/em&gt;: 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 &lt;em&gt;m&lt;/em&gt;-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
 

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