DIALS: implementation and evaluation of a new integration package

OLEX2 : a complete structure solution, refinement and analysis program

Dolomanov, O. V., Bourhis, L. J., Gildea, R. J., Howard, J. A. K., & Puschmann, H. (2009) · Journal of Applied Crystallography · doi:10.1107/s0021889808042726 · Cited by 32,811

SHELXT – Integrated space-group and crystal-structure determination

Sheldrick, G. M. (2015) · Acta Crystallographica Section A Foundations and Advances · doi:10.1107/s2053273314026370 · Cited by 29,831

PHENIX : a comprehensive Python-based system for macromolecular structure solution

Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716

Phaser crystallographic software

McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612

XDS

Kabsch, W. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909047337 · Cited by 16,463

Overview of the CCP 4 suite and current developments

Winn, M. D., Ballard, C. C., Cowtan, K. D., Dodson, E. J., Emsley, P., Evans, P. R., Keegan, R. M., Krissinel, E. B., Leslie, A. G. W., McCoy, A., et al. (2011) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910045749 · Cited by 12,353

Linking Crystallographic Model and Data Quality

Karplus, P. A., & Diederichs, K. (2012) · Science · doi:10.1126/science.1218231 · Cited by 1,781

SARS-CoV-2 neutralizing antibody structures inform therapeutic strategies

Barnes, C. O., Jette, C. A., Abernathy, M. E., Dam, K.-M. A., Esswein, S. R., Gristick, H. B., Malyutin, A. G., Sharaf, N. G., Huey-Tubman, K. E., Lee, Y. E., et al. (2020) · Nature · doi:10.1038/s41586-020-2852-1 · Cited by 1,599

SARS-CoV-2 Omicron-B.1.1.529 leads to widespread escape from neutralizing antibody responses

Dejnirattisai, W., Huo, J., Zhou, D., Zahradník, J., Supasa, P., Liu, C., Duyvesteyn, H. M. E., Ginn, H. M., Mentzer, A. J., Tuekprakhon, A., et al. (2022) · Cell · doi:10.1016/j.cell.2021.12.046 · Cited by 930

Reduced neutralization of SARS-CoV-2 B.1.617 by vaccine and convalescent serum

Liu, C., Ginn, H. M., Dejnirattisai, W., Supasa, P., Wang, B., Tuekprakhon, A., Nutalai, R., Zhou, D., Mentzer, A. J., Zhao, Y., et al. (2021) · Cell · doi:10.1016/j.cell.2021.06.020 · Cited by 669

Antibody evasion by the P.1 strain of SARS-CoV-2

Dejnirattisai, W., Zhou, D., Supasa, P., Liu, C., Mentzer, A. J., Ginn, H. M., Zhao, Y., Duyvesteyn, H. M. E., Tuekprakhon, A., Nutalai, R., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.055 · Cited by 583

Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera

Supasa, P., Zhou, D., Dejnirattisai, W., Liu, C., Mentzer, A. J., Ginn, H. M., Zhao, Y., Duyvesteyn, H. M. E., Nutalai, R., Tuekprakhon, A., et al. (2021) · Cell · doi:10.1016/j.cell.2021.02.033 · Cited by 460

The antigenic anatomy of SARS-CoV-2 receptor binding domain

Dejnirattisai, W., Zhou, D., Ginn, H. M., Duyvesteyn, H. M. E., Supasa, P., Case, J. B., Zhao, Y., Walter, T. S., Mentzer, A. J., Liu, C., et al. (2021) · Cell · doi:10.1016/j.cell.2021.02.032 · Cited by 371

Structural basis for the neutralization of SARS-CoV-2 by an antibody from a convalescent patient

Zhou, D., Duyvesteyn, H. M. E., Chen, C.-P., Huang, C.-G., Chen, T.-H., Shih, S.-R., Lin, Y.-C., Cheng, C.-Y., Cheng, S.-H., Huang, Y.-C., et al. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0480-y · Cited by 274

Structural basis of indisulam-mediated RBM39 recruitment to DCAF15 E3 ligase complex

Bussiere, D. E., Xie, L., Srinivas, H., Shu, W., Burke, A., Be, C., Zhao, J., Godbole, A., King, D., Karki, R. G., et al. (2020) · Nature Chemical Biology · doi:10.1038/s41589-019-0411-6 · Cited by 257

Asgard archaea shed light on the evolutionary origins of the eukaryotic ubiquitin-ESCRT machinery

Hatano, T., Palani, S., Papatziamou, D., Salzer, R., Souza, D. P., Tamarit, D., Makwana, M., Potter, A., Haig, A., Xu, W., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-30656-2 · Cited by 104

Mining the CRBN target space redefines rules for molecular glue-induced neosubstrate recognition

Petzold, G., Gainza, P., Annunziato, S., Lamberto, I., Trenh, P., McAllister, L. A., DeMarco, B., Schwander, L., Bunker, R. D., Zlotosch, M., et al. (2025) · Science · doi:10.1126/science.adt6736 · Cited by 117

Structural basis of BRCC36 function in DNA repair and immune regulation

Rabl, J., Bunker, R. D., Schenk, A. D., Cavadini, S., Gill, M. E., Abdulrahman, W., Andrés-Pons, A., Luijsterburg, M. S., Ibrahim, A. F. M., Branigan, E., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.06.002 · Cited by 84

Structure-based evolution of a promiscuous inhibitor to a selective stabilizer of protein–protein interactions

Sijbesma, E., Visser, E., Plitzko, K., Thiel, P., Milroy, L.-G., Kaiser, M., Brunsveld, L., & Ottmann, C. (2020) · Nature Communications · doi:10.1038/s41467-020-17741-0 · Cited by 72

Accurate modeling of peptide-MHC structures with AlphaFold

Mikhaylov, V., Brambley, C. A., Keller, G. L. J., Arbuiso, A. G., Weiss, L. I., Baker, B. M., & Levine, A. J. (2024) · Structure · doi:10.1016/j.str.2023.11.011 · Cited by 72

Computational design of sequence-specific DNA-binding proteins

Glasscock, C. J., Pecoraro, R. J., McHugh, R., Doyle, L. A., Chen, W., Boivin, O., Lonnquist, B., Na, E., Politanska, Y., Haddox, H. K., et al. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-025-01669-4 · Cited by 58

The MTR4 helicase recruits nuclear adaptors of the human RNA exosome using distinct arch-interacting motifs

Lingaraju, M., Johnsen, D., Schlundt, A., Langer, L. M., Basquin, J., Sattler, M., Heick Jensen, T., Falk, S., & Conti, E. (2019) · Nature Communications · doi:10.1038/s41467-019-11339-x · Cited by 55

Fragment-based computational design of antibodies targeting structured epitopes

Aguilar Rangel, M., Bedwell, A., Costanzi, E., Taylor, R. J., Russo, R., Bernardes, G. J. L., Ricagno, S., Frydman, J., Vendruscolo, M., & Sormanni, P. (2022) · Science Advances · doi:10.1126/sciadv.abp9540 · Cited by 55

Design of a Cereblon construct for crystallographic and biophysical studies of protein degraders

Kroupova, A., Spiteri, V. A., Rutter, Z. J., Furihata, H., Darren, D., Ramachandran, S., Chakraborti, S., Haubrich, K., Pethe, J., Gonzales, D., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-52871-9 · Cited by 47

Antibacterial T6SS effectors with a VRR-Nuc domain are structure-specific nucleases

Hespanhol, J. T., Sanchez-Limache, D. E., Nicastro, G. G., Mead, L., Llontop, E. E., Chagas-Santos, G., Farah, C. S., de Souza, R. F., Galhardo, R. D. S., Lovering, A. L., et al. (2022) · eLife · doi:10.7554/elife.82437 · Cited by 45

De novo designed peptides for cellular delivery and subcellular localisation

Rhys, G. G., Cross, J. A., Dawson, W. M., Thompson, H. F., Shanmugaratnam, S., Savery, N. J., Dodding, M. P., Höcker, B., & Woolfson, D. N. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-01076-6 · Cited by 44

GPR97 triggers inflammatory processes in human neutrophils via a macromolecular complex upstream of PAR2 activation

Chu, T.-Y., Zheng-Gérard, C., Huang, K.-Y., Chang, Y.-C., Chen, Y.-W., I, K.-Y., Lo, Y.-L., Chiang, N.-Y., Chen, H.-Y., Stacey, M., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34083-1 · Cited by 37

Uncovering an allosteric mode of action for a selective inhibitor of human Bloom syndrome protein

Chen, X., Ali, Y. I., Fisher, C. E., Arribas-Bosacoma, R., Rajasekaran, M. B., Williams, G., Walker, S., Booth, J. R., Hudson, J. J., Roe, S. M., et al. (2021) · eLife · doi:10.7554/elife.65339 · Cited by 34

Structure of the malaria vaccine candidate Pfs48/45 and its recognition by transmission blocking antibodies

Ko, K.-T., Lennartz, F., Mekhaiel, D., Guloglu, B., Marini, A., Deuker, D. J., Long, C. A., Jore, M. M., Miura, K., Biswas, S., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-33379-6 · Cited by 32

De novo determination of mosquitocidal Cry11Aa and Cry11Ba structures from naturally-occurring nanocrystals

Tetreau, G., Sawaya, M. R., De Zitter, E., Andreeva, E. A., Banneville, A.-S., Schibrowsky, N. A., Coquelle, N., Brewster, A. S., Grünbein, M. L., Kovacs, G. N., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31746-x · Cited by 28

Bimodular architecture of bacterial effector SAP05 that drives ubiquitin-independent targeted protein degradation

(2023) · doi:10.1073/pnas.2310664120 · Cited by 27

Chimeric deubiquitinase engineering reveals structural basis for specific inhibition of the mitophagy regulator USP30

Kazi, N. H., Klink, N., Gallant, K., Kipka, G.-M., & Gersch, M. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-025-01534-4 · Cited by 25

Structural basis for IL-33 recognition and its antagonism by the helminth effector protein HpARI2

Jamwal, A., Colomb, F., McSorley, H. J., & Higgins, M. K. (2024) · Nature Communications · doi:10.1038/s41467-024-49550-0 · Cited by 15

Structural and regulatory insights into the glideosome-associated connector from Toxoplasma gondii

Kumar, A., Vadas, O., Dos Santos Pacheco, N., Zhang, X., Chao, K., Darvill, N., Rasmussen, H. Ø., Xu, Y., Lin, G. M.-H., Stylianou, F. A., et al. (2023) · eLife · doi:10.7554/elife.86049 · Cited by 15

The structure of an amyloid precursor protein/talin complex indicates a mechanical basis of Alzheimer’s disease

(2024) · doi:10.1098/rsob.240185 · Cited by 9

The crystal structure of vaccinia virus protein E2 and perspectives on the prediction of novel viral protein folds

(2022) · doi:10.1099/jgv.0.001716 · Cited by 8

Determinants of receptor tyrosine phosphatase homophilic adhesion: Structural comparison of PTPRK and PTPRM extracellular domains

Hay, I. M., Shamin, M., Caroe, E. R., Mohammed, A. S. A., Svergun, D. I., Jeffries, C. M., Graham, S. C., Sharpe, H. J., & Deane, J. E. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102750 · Cited by 7

Substrate recruitment via eIF2γ enhances catalytic efficiency of a holophosphatase that terminates the integrated stress response

Yan, Y., Shetty, M., Harding, H. P., George, G., Zyryanova, A., Labbé, K., Mafi, A., Hao, Q., Sidrauski, C., & Ron, D. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2320013121 · Cited by 7

Engineering of soluble bacteriorhodopsin

Nikolaev, A., Orlov, Y., Tsybrov, F., Kuznetsova, E., Shishkin, P., Kuzmin, A., Mikhailov, A., Nikolaeva, Y. S., Anuchina, A., Chizhov, I., et al. (2025) · Chemical Science · doi:10.1039/d5sc02453f · Cited by 6

Divergent polo boxes in KKT2 bind KKT1 to initiate the kinetochore assembly cascade in Trypanosoma brucei

Ishii, M., Ludzia, P., Marcianò, G., Allen, W., Nerusheva, O. O., & Akiyoshi, B. (2022) · Molecular Biology of the Cell · doi:10.1091/mbc.e22-07-0269-t · Cited by 5

Structure of the malaria vaccine candidate Pfs48/45 and its recognition by transmission blocking antibodies

Ko, K.-T., Lennartz, F., Mekhaiel, D., Guloglu, B., Marini, A., Deuker, D. J., Long, C. A., Jore, M. M., Miura, K., Biswas, S., et al. (2022) · doi:10.1101/2022.05.24.493318 · Cited by 4

Determinants of receptor tyrosine phosphatase homophilic adhesion: structural comparison of PTPRK and PTPRM extracellular domains

(2022) · doi:10.1101/2022.06.23.497309 · Cited by 1

Molecular mechanism and structural models of protein-mediated copper transfer to the Arabidopsis thaliana ethylene receptor ETR1 at the ER membrane

(2025) · doi:10.1038/s41598-025-19915-6 · Cited by 1

Molecular Mechanism and Structural Models of Protein-Mediated Copper Transfer to the Arabidopsis thaliana Ethylene Receptor ETR1 at the ER Membrane

Dluhosch, D., Kersten, L. S., Minges, A., Schott-Verdugo, S., Gohlke, H., & Groth, G. (2025) · doi:10.1101/2025.01.21.634023