The CCP4 suite: programs for protein crystallography

Mutant Ferritin L-chains That Cause Neurodegeneration Act in a Dominant-negative Manner to Reduce Ferritin Iron Incorporation

Luscieti, S., Santambrogio, P., Langlois d'Estaintot, B., Granier, T., Cozzi, A., Poli, M., Gallois, B., Finazzi, D., Cattaneo, A., Levi, S., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.096404 · Cited by 51

Cypher/ZASP Is a Novel A-kinase Anchoring Protein

Lin, C., Guo, X., Lange, S., Liu, J., Ouyang, K., Yin, X., Jiang, L., Cai, Y., Mu, Y., Sheikh, F., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.470708 · Cited by 55

Crystal Structure of an Archaeal Actin Homolog

Roeben, A., Kofler, C., Nagy, I., Nickell, S., Ulrich Hartl, F., & Bracher, A. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.01.096 · Cited by 53

High-resolution crystal structure of the restriction-modification controller protein C.AhdI from Aeromonas hydrophila

McGeehan, J. E., Streeter, S. D., Papapanagiotou, I., Fox, G. C., & Kneale, G. G. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.12.025 · Cited by 51

Structural Insight into Modest Binding of a Non-PXXP Ligand to the Signal Transducing Adaptor Molecule-2 Src Homology 3 Domain

Kaneko, T., Kumasaka, T., Ganbe, T., Sato, T., Miyazawa, K., Kitamura, N., & Tanaka, N. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306677200 · Cited by 51

Crystal Structure of the Tp34 (TP0971) Lipoprotein of Treponema pallidum

Deka, R. K., Brautigam, C. A., Tomson, F. L., Lumpkins, S. B., Tomchick, D. R., Machius, M., & Norgard, M. V. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610215200 · Cited by 50

Paying the Price of desolvation in solvent-exposed protein pockets: impact of distal solubilizing groups on affinity and binding thermodynamics in a series of thermolysin inhibitors.

Cramer, J., Krimmer, S. G., Heine, A., & Klebe, G. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00490 · Cited by 50

Model for Substrate Interactions in C5a Peptidase from Streptococcus pyogenes: a 1.9 Å Crystal Structure of the Active Form of ScpA.

Kagawa, T. F., O'Connell, M. R., Mouat, P., Paoli, M., O'Toole, P. W., & Cooney, J. C. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.12.074 · Cited by 50

X-Ray Crystallographic and Mutational Studies of Fluoroacetate Dehalogenase from Burkholderia sp. Strain FA1

Jitsumori, K., Omi, R., Kurihara, T., Kurata, A., Mihara, H., Miyahara, I., Hirotsu, K., & Esaki, N. (2009) · Journal of Bacteriology · doi:10.1128/jb.01654-08 · Cited by 50

1.2 Å crystal structure of the S. pneumoniae PhtA histidine triad domain a novel zinc binding fold

Riboldi-Tunnicliffe, A., Isaacs, N. W., & Mitchell, T. J. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.08.066 · Cited by 49

Crystal structures of MKK4 kinase domain reveal that substrate peptide binds to an allosteric site and induces an auto-inhibition state

Matsumoto, T., Kinoshita, T., Kirii, Y., Yokota, K., Hamada, K., & Tada, T. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.08.071 · Cited by 49

The Molecular Basis for Apolipoprotein E4 as the Major Risk Factor for Late-Onset Alzheimer's Disease

Raulin, A.-C., Kraft, L., Al-Hilaly, Y. K., Xue, W.-F., McGeehan, J. E., Atack, J. R., & Serpell, L. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.04.019 · Cited by 47

Protein structure determination by exhaustive search of Protein Data Bank derived databases

Stokes-Rees, I., & Sliz, P. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1012095107 · Cited by 45

Novel irreversible covalent BTK inhibitors discovered using DNA-encoded chemistry

Guilinger, J. P., Archna, A., Augustin, M., Bergmann, A., Centrella, P. A., Clark, M. A., Cuozzo, J. W., Däther, M., Guié, M.-A., Habeshian, S., et al. (2021) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2021.116223 · Cited by 49

Boca‐dependent maturation of β‐propeller/EGF modules in low‐density lipoprotein receptor proteins

Culi, J., Springer, T. A., & Mann, R. S. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600132 · Cited by 45

Functional analysis of human cytochrome P450 21A2 variants involved in congenital adrenal hyperplasia

Wang, C., Pallan, P. S., Zhang, W., Lei, L., Yoshimoto, F. K., Waterman, M. R., Egli, M., & Guengerich, F. P. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.792465 · Cited by 43

The Aspergillus fumigatus Sialidase Is a 3-Deoxy-d-glycero-d-galacto-2-nonulosonic Acid Hydrolase (KDNase)

Telford, J. C., Yeung, J. H. F., Xu, G., Kiefel, M. J., Watts, A. G., Hader, S., Chan, J., Bennet, A. J., Moore, M. M., & Taylor, G. L. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.207043 · Cited by 43

Structural hot spots determine functional diversity of the Candida glabrata epithelial adhesin family

Diderrich, R., Kock, M., Maestre-Reyna, M., Keller, P., Steuber, H., Rupp, S., Essen, L.-O., & Mösch, H.-U. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.655654 · Cited by 40

Role of a Conserved Glutamine Residue in Tuning the Catalytic Activity of Escherichia coli Cytochrome c Nitrite Reductase

Clarke, T. A., Kemp, G. L., Wonderen, J. H. V., Doyle, R.-M. A. S., Cole, J. A., Tovell, N., Cheesman, M. R., Butt, J. N., Richardson, D. J., & Hemmings, A. M. (2008) · Biochemistry · doi:10.1021/bi702175w · Cited by 40

Crystal Structures and RNA-binding Properties of the RNA Recognition Motifs of Heterogeneous Nuclear Ribonucleoprotein L

Zhang, W., Zeng, F., Liu, Y., Zhao, Y., Lv, H., Niu, L., Teng, M., & Li, X. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.463901 · Cited by 40

Structure of the GTPase-binding Domain of Sec5 and Elucidation of its Ral Binding Site

Mott, H. R., Nietlispach, D., Hopkins, L. J., Mirey, G., Camonis, J. H., & Owen, D. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300155200 · Cited by 39

Crystal structure of the C3bot–RalA complex reveals a novel type of action of a bacterial exoenzyme

Pautsch, A., Vogelsgesang, M., Tränkle, J., Herrmann, C., & Aktories, K. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600813 · Cited by 39

Structural Basis of the Interaction between Tuberous Sclerosis Complex 1 (TSC1) and Tre2-Bub2-Cdc16 Domain Family Member 7 (TBC1D7)

Qin, J., Wang, Z., Hoogeveen-Westerveld, M., Shen, G., Gong, W., Nellist, M., & Xu, W. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.701870 · Cited by 37

The atomic model of the human protective protein/cathepsin A suggests a structural basis for galactosialidosis

Rudenko, G., Bonten, E., Hol, W. G. J., & d’Azzo, A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.2.621 · Cited by 36

Structural Determination of Functional Domains in Early B-cell Factor (EBF) Family of Transcription Factors Reveals Similarities to Rel DNA-binding Proteins and a Novel Dimerization Motif

Siponen, M. I., Wisniewska, M., Lehtiö, L., Johansson, I., Svensson, L., Raszewski, G., Nilsson, L., Sigvardsson, M., & Berglund, H. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.c110.150482 · Cited by 34

Recognition of AT-Rich DNA Binding Sites by the MogR Repressor

Shen, A., Higgins, D. E., & Panne, D. (2009) · Structure · doi:10.1016/j.str.2009.02.018 · Cited by 35

Structure of NFAT Bound to DNA as a Monomer

Stroud, J. C., & Chen, L. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.09.065 · Cited by 35

Membrane catalysis of peptide–receptor bindingThis paper is one of a selection of papers published in this special issue entitled “Canadian Society of Biochemistry, Molecular & Cellular Biology 52nd Annual Meeting — Protein Folding: Principles and Diseases” and has undergone the Journal's usual peer review process.

Langelaan, D. N., & Rainey, J. K. (2010) · Biochemistry and Cell Biology · doi:10.1139/o09-129 · Cited by 35

The minor pilin PilV provides a conserved adhesion site throughout the antigenically variable meningococcal type IV pilus

Barnier, J.-P., Meyer, J., Kolappan, S., Bouzinba-Ségard, H., Gesbert, G., Jamet, A., Frapy, E., Schönherr-Hellec, S., Capel, E., Virion, Z., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2109364118 · Cited by 34

Molecular Architecture of the Ankyrin SOCS Box Family of Cul5-Dependent E3 Ubiquitin Ligases

Muniz, J. R. C., Guo, K., Kershaw, N. J., Ayinampudi, V., von Delft, F., Babon, J. J., & Bullock, A. N. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.06.015 · Cited by 34

The Third Conformation of p38α MAP Kinase Observed in Phosphorylated p38α and in Solution

Akella, R., Min, X., Wu, Q., Gardner, K. H., & Goldsmith, E. J. (2010) · Structure · doi:10.1016/j.str.2010.09.015 · Cited by 31

Fragment-Based Screening Maps Inhibitor Interactions in the ATP-Binding Site of Checkpoint Kinase 2

Silva-Santisteban, M. C., Westwood, I. M., Boxall, K., Brown, N., Peacock, S., McAndrew, C., Barrie, E., Richards, M., Mirza, A., Oliver, A. W., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0065689 · Cited by 31

Structure of the Bro1 Domain Protein BROX and Functional Analyses of the ALIX Bro1 Domain in HIV-1 Budding

Zhai, Q., Landesman, M. B., Robinson, H., Sundquist, W. I., & Hill, C. P. (2011) · PLoS ONE · doi:10.1371/journal.pone.0027466 · Cited by 31

Complex structure of the fission yeast SREBP-SCAP binding domains reveals an oligomeric organization

Gong, X., Qian, H., Shao, W., Li, J., Wu, J., Liu, J.-J., Li, W., Wang, H.-W., Espenshade, P., & Yan, N. (2016) · Cell Research · doi:10.1038/cr.2016.123 · Cited by 31

Structural analysis of haemoglobin binding by HpuA from the Neisseriaceae family

Wong, C. T., Xu, Y., Gupta, A., Garnett, J. A., Matthews, S. J., & Hare, S. A. (2015) · Nature Communications · doi:10.1038/ncomms10172 · Cited by 30

Immune Interference in Mycobacterium tuberculosis Intracellular Iron Acquisition through Siderocalin Recognition of Carboxymycobactins

Hoette, T. M., Clifton, M. C., Zawadzka, A. M., Holmes, M. A., Strong, R. K., & Raymond, K. N. (2011) · ACS Chemical Biology · doi:10.1021/cb200331g · Cited by 31

Structure of the Tuberous Sclerosis Complex 2 (TSC2) N Terminus Provides Insight into Complex Assembly and Tuberous Sclerosis Pathogenesis

Zech, R., Kiontke, S., Mueller, U., Oeckinghaus, A., & Kümmel, D. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.732446 · Cited by 29

Crystal structure of the MrkD1P receptor binding domain of Klebsiella pneumoniae and identification of the human collagen V binding interface

Rêgo, A. T., Johnson, J. G., Geibel, S., Enguita, F. J., Clegg, S., & Waksman, G. (2012) · Molecular Microbiology · doi:10.1111/mmi.12023 · Cited by 29

On the Structure and Dynamics of Duplex GNA

Johnson, A. T., Schlegel, M. K., Meggers, E., Essen, L.-O., & Wiest, O. (2011) · The Journal of Organic Chemistry · doi:10.1021/jo201469b · Cited by 28

Crystal structure of the yeast TSC1 core domain and implications for tuberous sclerosis pathological mutations

Sun, W., Zhu, Y. J., Wang, Z., Zhong, Q., Gao, F., Lou, J., Gong, W., & Xu, W. (2013) · Nature Communications · doi:10.1038/ncomms3135 · Cited by 27

Structural characterization and AlphaFold modeling of human T cell receptor recognition of NRAS cancer neoantigens

Wu, D., Yin, R., Chen, G., Ribeiro-Filho, H. V., Cheung, M., Robbins, P. F., Mariuzza, R. A., & Pierce, B. G. (2024) · Science Advances · doi:10.1126/sciadv.adq6150 · Cited by 27

Mechanism of N10‐formyltetrahydrofolate synthetase derived from complexes with intermediates and inhibitors

Celeste, L. R., Chai, G., Bielak, M., Minor, W., Lovelace, L. L., & Lebioda, L. (2012) · Protein Science · doi:10.1002/pro.2005 · Cited by 27

Ubiquitous purine sensor modulates diverse signal transduction pathways in bacteria

Monteagudo-Cascales, E., Gumerov, V. M., Fernández, M., Matilla, M. A., Gavira, J. A., Zhulin, I. B., & Krell, T. (2024) · Nature Communications · doi:10.1038/s41467-024-50275-3 · Cited by 27

The metastability of human UDP-galactose 4′-epimerase (GALE) is increased by variants associated with type III galactosemia but decreased by substrate and cofactor binding

Pey, A. L., Padín-Gonzalez, E., Mesa-Torres, N., & Timson, D. J. (2014) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2014.07.030 · Cited by 26

Alpha-1 Giardin is an Annexin with Highly Unusual Calcium-Regulated Mechanisms

Weeratunga, S. K., Osman, A., Hu, N.-J., Wang, C. K., Mason, L., Svärd, S., Hope, G., Jones, M. K., & Hofmann, A. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.06.041 · Cited by 26

Evolution of Enzymatic Activities in the Enolase Superfamily: Identification of the General Acid Catalyst in theActive Site of d-Glucarate Dehydratase from Escherichia coli,

Gulick, A. M., Hubbard, B. K., Gerlt, J. A., & Rayment, I. (2001) · Biochemistry · doi:10.1021/bi010733b · Cited by 25

RhoGDIα Acetylation at K127 and K141 Affects Binding toward Nonprenylated RhoA

Kuhlmann, N., Wroblowski, S., Scislowski, L., & Lammers, M. (2016) · Biochemistry · doi:10.1021/acs.biochem.5b01242 · Cited by 24

Protein dynamics at Eph receptor-ligand interfaces as revealed by crystallography, NMR and MD simulations

Qin, H., Lim, L., & Song, J. (2012) · BMC Biophysics · doi:10.1186/2046-1682-5-2 · Cited by 23

Structural and functional characterization of Schistosoma mansoni Thioredoxin

Boumis, G., Angelucci, F., Bellelli, A., Brunori, M., Dimastrogiovanni, D., & Miele, A. E. (2011) · Protein Science · doi:10.1002/pro.634 · Cited by 23

The Structural Differences between a Glycoprotein Specific F-Box Protein Fbs1 and Its Homologous Protein FBG3

Kumanomidou, T., Nishio, K., Takagi, K., Nakagawa, T., Suzuki, A., Yamane, T., Tokunaga, F., Iwai, K., Murakami, A., Yoshida, Y., et al. (2015) · PLOS ONE · doi:10.1371/journal.pone.0140366 · Cited by 21

An Open and Shut Case: The Interaction of Magnesium with MST Enzymes

Meneely, K. M., Sundlov, J. A., Gulick, A. M., Moran, G. R., & Lamb, A. L. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b05134 · Cited by 20

Unique Structure and Dynamics of the EphA5 Ligand Binding Domain Mediate Its Binding Specificity as Revealed by X-ray Crystallography, NMR and MD Simulations

Huan, X., Shi, J., Lim, L., Mitra, S., Zhu, W., Qin, H., Pasquale, E. B., & Song, J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0074040 · Cited by 16

Crystal and solution structures disclose a putative transient state of mitogen-activated protein kinase kinase 4

Matsumoto, T., Kinoshita, T., Kirii, Y., Tada, T., & Yamano, A. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.07.066 · Cited by 15

AlphaFold accurately predicts distinct conformations based on the oligomeric state of a de novo designed protein

Cummins, M. C., Jacobs, T. M., Teets, F. D., DiMaio, F., Tripathy, A., & Kuhlman, B. (2022) · Protein Science · doi:10.1002/pro.4368 · Cited by 15

Designed Ankyrin Repeat Proteins provide insights into the structure and function of CagI and are potent inhibitors of CagA translocation by the Helicobacter pylori type IV secretion system

Blanc, M., Lettl, C., Guérin, J., Vieille, A., Furler, S., Briand-Schumacher, S., Dreier, B., Bergé, C., Plückthun, A., Vadon-Le Goff, S., et al. (2023) · PLOS Pathogens · doi:10.1371/journal.ppat.1011368 · Cited by 9

Interfacial water confers transcription factors with dinucleotide specificity

(2025) · doi:10.1038/s41594-024-01449-6 · Cited by 11

PTRAMP, CSS and Ripr form a conserved complex required for merozoite invasion of Plasmodium species into erythrocytes

(2026) · doi:10.1038/s41467-026-68486-1 · Cited by 10

Structural journey of an insecticidal protein against western corn rootworm

Marini, G., Poland, B., Leininger, C., Lukoyanova, N., Spielbauer, D., Barry, J. K., Altier, D., Lum, A., Scolaro, E., Ortega, C. P., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-39891-7 · Cited by 9

Structural and mechanistic analysis of covalent ligands targeting the RNA-binding protein NONO

Lindsey, G. L., Hockley, T. K., Gomez, A. V., Marshall, A. C., Brothers, W. R., Finney, C. T., Gross, J., Fox, A. H., Yeo, G. W., Melillo, B., et al. (2026) · Cell Chemical Biology · doi:10.1016/j.chembiol.2025.12.010 · Cited by 6

The structure of KPN03535 (gi|152972051), a novel putative lipoprotein from Klebsiella pneumoniae, reveals an OB-fold

Das, D., Kozbial, P., Han, G. W., Carlton, D., Jaroszewski, L., Abdubek, P., Astakhova, T., Axelrod, H. L., Bakolitsa, C., Chen, C., et al. (2010) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309109018168 · Cited by 2

Structural and functional basis of PU.1-BAF interaction enables targeting of lineage-specific transcription

Sadalge, D., Clasman, J. R., Topal, S., Musser, D., Von der Porten, L., Wu, S., Schultz, S. E., Austin, W., Huang, D., Gao, Y.-D., et al. (2025) · doi:10.1101/2025.08.01.667454 · Cited by 2

A small molecule PTER-selective inhibitor reduces food intake and body weight

Fu, S., Wang, L., Li, V. L., Lyu, X., Wei, W., Shi, X., Deng, S., Barber, J. L., Tahir, U. A., Adams, C., et al. (2026) · Cell Chemical Biology · doi:10.1016/j.chembiol.2026.02.005 · Cited by 2

A small molecule PTER-selective inhibitor reduces food intake and body weight

Fu, S., Wang, L., Li, V. L., Lyu, X., Wei, W., Shi, X., Deng, S., Barber, J. L., Tahir, U. A., Adams, C., et al. (2026) · doi:10.64898/2026.01.26.701829 · Cited by 2

Reprogramming of bacterial virulence by lysine acetylation

Schmöker, O., Girbardt, B., Schulze, S., Palm, G. J., Berndt, L., Hoppen, J., Kara, N., Schöps, X., Al-Abdulla, R., Garz, K., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-72244-8 · Cited by 2