The integration of macromolecular diffraction data

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

Crystal Structure of Agaricus bisporus Mushroom Tyrosinase: Identity of the Tetramer Subunits and Interaction with Tropolone

Ismaya, W. T., Rozeboom, H. J., Weijn, A., Mes, J. J., Fusetti, F., Wichers, H. J., & Dijkstra, B. W. (2011) · Biochemistry · doi:10.1021/bi200395t · Cited by 872

Targeting C-reactive protein for the treatment of cardiovascular disease.

Pepys, M. B., Hirschfield, G. M., Tennent, G. A., Ruth Gallimore, J., Kahan, M. C., Bellotti, V., Hawkins, P. N., Myers, R. M., Smith, M. D., Polara, A., et al. (2006) · Nature · doi:10.1038/nature04672 · Cited by 672

Bioenergetic cost of making an adenosine triphosphate molecule in animal mitochondria

Watt, I. N., Montgomery, M. G., Runswick, M. J., Leslie, A. G. W., & Walker, J. E. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1011099107 · Cited by 513

A small-molecule inhibitor of the ubiquitin activating enzyme for cancer treatment

Hyer, M. L., Milhollen, M. A., Ciavarri, J., Fleming, P., Traore, T., Sappal, D., Huck, J., Shi, J., Gavin, J., Brownell, J., et al. (2018) · Nature Medicine · doi:10.1038/nm.4474 · Cited by 447

The Molecular Basis for the Endocytosis of Small R-SNAREs by the Clathrin Adaptor CALM

Miller, S. E., Sahlender, D. A., Graham, S. C., Höning, S., Robinson, M. S., Peden, A. A., & Owen, D. J. (2011) · Cell · doi:10.1016/j.cell.2011.10.038 · Cited by 192

Structural basis for the assembly of the SMRT/NCoR core transcriptional repression machinery

Oberoi, J., Fairall, L., Watson, P. J., Yang, J.-C., Czimmerer, Z., Kampmann, T., Goult, B. T., Greenwood, J. A., Gooch, J. T., Kallenberger, B. C., et al. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1983 · Cited by 165

Molecular basis for SH3 domain regulation of F-BAR–mediated membrane deformation

Rao, Y., Ma, Q., Vahedi-Faridi, A., Sundborger, A., Pechstein, A., Puchkov, D., Luo, L., Shupliakov, O., Saenger, W., & Haucke, V. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1003478107 · Cited by 149

Crystal structures of mammalian glutamine synthetases illustrate substrate-induced conformational changes and provide opportunities for drug and herbicide design

Krajewski, W. W., Collins, R., Holmberg-Schiavone, L., Jones, T. A., Karlberg, T., & Mowbray, S. L. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.10.029 · Cited by 135

Repulsive guidance molecule is a structural bridge between neogenin and bone morphogenetic protein

Healey, E. G., Bishop, B., Elegheert, J., Bell, C. H., Padilla-Parra, S., & Siebold, C. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3016 · Cited by 112

The structure of the KtrAB potassium transporter

Vieira-Pires, R. S., Szollosi, A., & Morais-Cabral, J. H. (2013) · Nature · doi:10.1038/nature12055 · Cited by 109

The high-resolution crystal structure of periplasmic Haemophilus influenzae NAD nucleotidase reveals a novel enzymatic function of human CD73 related to NAD metabolism

Garavaglia, S., Bruzzone, S., Cassani, C., Canella, L., Allegrone, G., Sturla, L., Mannino, E., Millo, E., De Flora, A., & Rizzi, M. (2012) · Biochemical Journal · doi:10.1042/bj20111263 · Cited by 94

Recognition of protein-linked glycans as a determinant of peptidase activity

Noach, I., Ficko-Blean, E., Pluvinage, B., Stuart, C., Jenkins, M. L., Brochu, D., Buenbrazo, N., Wakarchuk, W., Burke, J. E., Gilbert, M., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1615141114 · Cited by 89

Regulation of RXR-RAR Heterodimers by RXR- and RAR-Specific Ligands and Their Combinations

le Maire, A., Teyssier, C., Balaguer, P., Bourguet, W., & Germain, P. (2019) · Cells · doi:10.3390/cells8111392 · Cited by 88

The IDOL-UBE2D complex mediates sterol-dependent degradation of the LDL receptor

Zhang, L., Fairall, L., Goult, B. T., Calkin, A. C., Hong, C., Millard, C. J., Tontonoz, P., & Schwabe, J. W. R. (2011) · Genes & Development · doi:10.1101/gad.2056211 · Cited by 86

Assembly and solution structure of the core retromer protein complex

Norwood, S. J., Shaw, D. J., Cowieson, N. P., Owen, D. J., Teasdale, R. D., & Collins, B. M. (2011) · Traffic · doi:10.1111/j.1600-0854.2010.01124.x · Cited by 84

Structural Characterization of the Tetrameric form of the Major Cat Allergen Fel d 1

Kaiser, L., Velickovic, T. C., Badia-Martinez, D., Adedoyin, J., Thunberg, S., Hallén, D., Berndt, K., Grönlund, H., Gafvelin, G., van Hage, M., et al. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.04.074 · Cited by 70

Crystal structure of Escherichia coli alkanesulfonate monooxygenase SsuD

Eichhorn, E., Davey, C. A., Sargent, D. F., Leisinger, T., & Richmond, T. J. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)01069-0 · Cited by 57

High-Resolution Crystal Structure of the Subclass B3 Metallo-β-Lactamase BJP-1: Rational Basis for Substrate Specificity and Interaction with Sulfonamides

Docquier, J.-D., Benvenuti, M., Calderone, V., Stoczko, M., Menciassi, N., Rossolini, G. M., & Mangani, S. (2010) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00409-10 · Cited by 51

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

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

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

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

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

Substrate Trapping in Polyketide Synthase Thioesterase Domains: Structural Basis for Macrolactone Formation

McCullough, T. M., Choudhary, V., Akey, D. L., Skiba, M. A., Bernard, S. M., Kittendorf, J. D., Schmidt, J. J., Sherman, D. H., & Smith, J. L. (2024) · ACS Catalysis · doi:10.1021/acscatal.4c03637 · Cited by 8

Mutant structure of metabolic switch protein in complex with monomeric c-di-GMP reveals a potential mechanism of protein-mediated ligand dimerization

Dubey, B. N., Shyp, V., Fucile, G., Sondermann, H., Jenal, U., & Schirmer, T. (2023) · Scientific Reports · doi:10.1038/s41598-023-29110-0 · Cited by 2