The CCP4 suite: programs for protein crystallography

Collaborative Computational Project, Number 4·1994·Acta Crystallographica Section D Biological Crystallography

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Abstract

The CCP4 (Collaborative Computational Project, number 4) program suite is a collection of programs and associated data and subroutine libraries which can be used for macromolecular structure determination by X-ray crystallography. The suite is designed to be flexible, allowing users a number of methods of achieving their aims and so there may be more than one program to cover each function. The programs are written mainly in standard Fortran77. They are from a wide variety of sources but are connected by standard data file formats. The package has been ported to all the major platforms under both Unix and VMS. The suite is distributed by anonymous ftp from Daresbury Laboratory and is widely used throughout the world.

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Leduc, A.-M., Trent, J. O., Wittliff, J. L., Bramlett, K. S., Briggs, S. L., Chirgadze, N. Y., Wang, Y., Burris, T. P., & Spatola, A. F. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1934759100 · Cited by 222
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Brotherton, D. H., Dhanaraj, V., Wick, S., Brizuela, L., Domaille, P. J., Volyanik, E., Xu, X., Parisini, E., Smith, B. O., Archer, S. J., et al. (1998) · Nature · doi:10.1038/26164 · Cited by 210
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Snyder, J. T., Worthylake, D. K., Rossman, K. L., Betts, L., Pruitt, W. M., Siderovski, D. P., Der, C. J., & Sondek, J. (2002) · Nature Structural Biology · doi:10.1038/nsb796 · Cited by 209
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Shimizu, H., Tosaki, A., Kaneko, K., Hisano, T., Sakurai, T., & Nukina, N. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.02185-07 · Cited by 205
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Ely, L. K., Fischer, S., & Garcia, K. C. (2009) · Nature Immunology · doi:10.1038/ni.1813 · Cited by 195
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Wang, H., Klein, M. G., Zou, H., Lane, W., Snell, G., Levin, I., Li, K., & Sang, B.-C. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3049 · Cited by 192
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Willows, R., Sanders, M. J., Xiao, B., Patel, B. R., Martin, S. R., Read, J., Wilson, J. R., Hubbard, J., Gamblin, S. J., & Carling, D. (2017) · Biochemical Journal · doi:10.1042/bcj20170458 · Cited by 190
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Oliveira, T. F., Vonrhein, C., Matias, P. M., Venceslau, S. S., Pereira, I. A. C., & Archer, M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805643200 · Cited by 190
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Hayes, R. P., Xiao, Y., Ding, F., van Erp, P. B. G., Rajashankar, K., Bailey, S., Wiedenheft, B., & Ke, A. (2016) · Nature · doi:10.1038/nature16995 · Cited by 187
CR8, a potent and selective, roscovitine-derived inhibitor of cyclin-dependent kinases
Bettayeb, K., Oumata, N., Echalier, A., Ferandin, Y., Endicott, J. A., Galons, H., & Meijer, L. (2008) · Oncogene · doi:10.1038/onc.2008.191 · Cited by 184
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Crystal structure of SIV matrix antigen and implications for virus assembly
Rao, Z., Belyaev, A. S., Fry, E., Roy, P., Jones, I. M., & Stuart, D. I. (1995) · Nature · doi:10.1038/378743a0 · Cited by 183
Crystal structure of the carbohydrate recognition domain of the H1 subunit of the asialoglycoprotein receptor
Meier, M., Bider, M. D., Malashkevich, V. N., Spiess, M., & Burkhard, P. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3853 · Cited by 182
Structure of the metal-ion-activated diphtheria toxin repressor/ tox operator complex
White, A., Ding, X., vanderSpek, J. C., Murphy, J. R., & Ringe, D. (1998) · Nature · doi:10.1038/28893 · Cited by 180
Molecular Structure of Human TFIIH
Schultz, P., Fribourg, S., Poterszman, A., Mallouh, V., Moras, D., & Egly, J. M. (2000) · Cell · doi:10.1016/s0092-8674(00)00082-9 · Cited by 180
X-ray structure of a native calicivirus: Structural insights into antigenic diversity and host specificity
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Phan, J., Li, Z., Kasprzak, A., Li, B., Sebti, S., Guida, W., Schönbrunn, E., & Chen, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.073056 · Cited by 173
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Masuda, M., Uno, Y., Ohbayashi, N., Ohata, H., Mimata, A., Kukimoto-Niino, M., Moriyama, H., Kashimoto, S., Inoue, T., Goto, N., et al. (2016) · Nature Communications · doi:10.1038/ncomms12586 · Cited by 168
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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
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Grigg, J. C., Vermeiren, C. L., Heinrichs, D. E., & Murphy, M. E. P. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05502.x · Cited by 166
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Structural insights into the assembly and activation of IL-1β with its receptors
Wang, D., Zhang, S., Li, L., Liu, X., Mei, K., & Wang, X. (2010) · Nature Immunology · doi:10.1038/ni.1925 · Cited by 162
NFκB selectivity of estrogen receptor ligands revealed by comparative crystallographic analyses
Nettles, K. W., Bruning, J. B., Gil, G., Nowak, J., Sharma, S. K., Hahm, J. B., Kulp, K., Hochberg, R. B., Zhou, H., Katzenellenbogen, J. A., et al. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.76 · Cited by 159
p66α–MBD2 coiled-coil interaction and recruitment of Mi-2 are critical for globin gene silencing by the MBD2–NuRD complex
Gnanapragasam, M. N., Scarsdale, J. N., Amaya, M. L., Webb, H. D., Desai, M. A., Walavalkar, N. M., Wang, S. Z., Zu Zhu, S., Ginder, G. D., & Williams, D. C. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1015341108 · Cited by 148
Structural and Energetic Mechanisms of Cooperative Autoinhibition and Activation of Vav1
Yu, B., Martins, I. R. S., Li, P., Amarasinghe, G. K., Umetani, J., Fernandez-Zapico, M. E., Billadeau, D. D., Machius, M., Tomchick, D. R., & Rosen, M. K. (2010) · Cell · doi:10.1016/j.cell.2009.12.033 · Cited by 156
Crystal structure of a membrane-embedded H+-translocating pyrophosphatase
Lin, S.-M., Tsai, J.-Y., Hsiao, C.-D., Huang, Y.-T., Chiu, C.-L., Liu, M.-H., Tung, J.-Y., Liu, T.-H., Pan, R.-L., & Sun, Y.-J. (2012) · Nature · doi:10.1038/nature10963 · Cited by 156
Phosphorylation-dependent interaction between antigenic peptides and MHC class I: a molecular basis for the presentation of transformed self
Mohammed, F., Cobbold, M., Zarling, A. L., Salim, M., Barrett-Wilt, G. A., Shabanowitz, J., Hunt, D. F., Engelhard, V. H., & Willcox, B. E. (2008) · Nature Immunology · doi:10.1038/ni.1660 · Cited by 155
Inter- and Intragenus Structural Variations in Caliciviruses and Their Functional Implications
Chen, R., Neill, J. D., Noel, J. S., Hutson, A. M., Glass, R. I., Estes, M. K., & Prasad, B. V. V. (2004) · Journal of Virology · doi:10.1128/jvi.78.12.6469-6479.2004 · Cited by 154
Crystal Structure and Deletion Analysis Show that the Accessory Subunit of Mammalian DNA Polymerase γ, PolγB, Functions as a Homodimer
Carrodeguas, J. A., Theis, K., Bogenhagen, D. F., & Kisker, C. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00153-8 · Cited by 150
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Arnoux, P., Sabaty, M., Alric, J., Frangioni, B., Guigliarelli, B., Adriano, J.-M., & Pignol, D. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb994 · Cited by 149
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
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Kawano, S., Tamura, Y., Kojima, R., Bala, S., Asai, E., Michel, A. H., Kornmann, B., Riezman, I., Riezman, H., Sakae, Y., et al. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201704119 · Cited by 148
“To monitor lipid transfer between liposomes via the HMmm1s– Mdm12 complex and MBP-HMmm1s, we adopted fluorescent dequenching assays as described previously (Connerth et al., 2012; Watanabe et al., 2015; Miyata et al., 2016).”
Method
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Montaño, S. P., Pigli, Y. Z., & Rice, P. A. (2012) · Nature · doi:10.1038/nature11602 · Cited by 137
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Vogtherr, M., Saxena, K., Hoelder, S., Grimme, S., Betz, M., Schieborr, U., Pescatore, B., Robin, M., Delarbre, L., Langer, T., et al. (2006) · Angewandte Chemie International Edition · doi:10.1002/anie.200502770 · Cited by 145
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Bubeck, D., Reijns, M. A. M., Graham, S. C., Astell, K. R., Jones, E. Y., & Jackson, A. P. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkq980 · Cited by 144
Coupling of receptor conformation and ligand orientation determine graded activity
Bruning, J. B., Parent, A. A., Gil, G., Zhao, M., Nowak, J., Pace, M. C., Smith, C. L., Afonine, P. V., Adams, P. D., Katzenellenbogen, J. A., et al. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.451 · Cited by 142
New aspects of electron transfer revealed by the crystal structure of a truncated bovine adrenodoxin, Adx(4-108)
Müller, A., Müller, J. J., Muller, Y. A., Uhlmann, H., Bernhardt, R., & Heinemann, U. (1998) · Structure · doi:10.1016/s0969-2126(98)00031-8 · Cited by 142
Structural and Functional Analysis of a Conjugated Bile Salt Hydrolase from Bifidobacterium longum Reveals an Evolutionary Relationship with Penicillin V Acylase
Kumar, R. S., Brannigan, J. A., Prabhune, A. A., Pundle, A. V., Dodson, G. G., Dodson, E. J., & Suresh, C. G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604172200 · Cited by 143

Authors: Collaborative Computational Project, N. 4.
Venue: Acta Crystallographica Section D Biological Crystallography
Publisher: International Union of Crystallography (IUCr)
Published: 1994-09-01
Volume: 50
Issue: 5
Pages: 760-763
ISSN: 0907-4449 (ISSN-L)
DOI: 10.1107/s0907444994003112
OpenAlex: W2001641653
Cited by: 17,270
References: 0
FWCI: 199.16
Type: journal article
Language: en
Open access: closed

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The CCP4 suite: programs for protein crystallography

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