AMoRe: an automated package for molecular replacement

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

X-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity

Dutzler, R., Campbell, E. B., Cadene, M., Chait, B. T., & MacKinnon, R. (2002) · Nature · doi:10.1038/415287a · Cited by 1,446

Molecular Architecture of the Rotary Motor in ATP Synthase

Stock, D., Leslie, A. G. W., & Walker, J. E. (1999) · Science · doi:10.1126/science.286.5445.1700 · Cited by 1,271

Complete Structure of the 11-Subunit Bovine Mitochondrial Cytochrome bc 1 Complex

Iwata, S., Lee, J. W., Okada, K., Lee, J. K., Iwata, M., Rasmussen, B., Link, T. A., Ramaswamy, S., & Jap, B. K. (1998) · Science · doi:10.1126/science.281.5373.64 · Cited by 1,253

Structure of mammalian AMPK and its regulation by ADP

Xiao, B., Sanders, M. J., Underwood, E., Heath, R., Mayer, F. V., Carmena, D., Jing, C., Walker, P. A., Eccleston, J. F., Haire, L. F., et al. (2011) · Nature · doi:10.1038/nature09932 · Cited by 926

Shiga-like toxins are neutralized by tailored multivalent carbohydrate ligands

Kitov, P. I., Sadowska, J. M., Mulvey, G., Armstrong, G. D., Ling, H., Pannu, N. S., Read, R. J., & Bundle, D. R. (2000) · Nature · doi:10.1038/35001095 · Cited by 869

The crystal structure of the nuclear receptor for vitamin D bound to its natural ligand

Rochel, N., Wurtz, J. M., Mitschler, A., Klaholz, B., & Moras, D. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80413-x · Cited by 842

The physiological structure of human C-reactive protein and its complex with phosphocholine

Thompson, D., Pepys, M. B., & Wood, S. P. (1999) · Structure · doi:10.1016/s0969-2126(99)80023-9 · Cited by 818

ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer

Smith, P. C., Karpowich, N., Millen, L., Moody, J. E., Rosen, J., Thomas, P. J., & Hunt, J. F. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00576-2 · Cited by 773

Structural definition of a conserved neutralization epitope on HIV-1 gp120

Zhou, T., Xu, L., Dey, B., Hessell, A. J., Van Ryk, D., Xiang, S.-H., Yang, X., Zhang, M.-Y., Zwick, M. B., Arthos, J., et al. (2007) · Nature · doi:10.1038/nature05580 · Cited by 770

Activation mechanism of the MAP kinase ERK2 by dual phosphorylation

Canagarajah, B. J., Khokhlatchev, A., Cobb, M. H., & Goldsmith, E. J. (1997) · Cell · doi:10.1016/s0092-8674(00)80351-7 · Cited by 729

Gating the Selectivity Filter in ClC Chloride Channels

Dutzler, R., Campbell, E. B., & MacKinnon, R. (2003) · Science · doi:10.1126/science.1082708 · Cited by 727

Crystal Structure of Human Cyclophilin A Bound to the Amino-Terminal Domain of HIV-1 Capsid

Gamble, T. R., Vajdos, F. F., Yoo, S., Worthylake, D. K., Houseweart, M., Sundquist, W. I., & Hill, C. P. (1996) · Cell · doi:10.1016/s0092-8674(00)81823-1 · Cited by 706

High-affinity binders selected from designed ankyrin repeat protein libraries

Binz, H. K., Amstutz, P., Kohl, A., Stumpp, M. T., Briand, C., Forrer, P., Grütter, M. G., & Plückthun, A. (2004) · Nature Biotechnology · doi:10.1038/nbt962 · Cited by 656

Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1.

Gomis-R¨th, F.-X., Maskos, K., Betz, M., Bergner, A., Huber, R., Suzuki, K., Yoshida, N., Nagase, H., Brew, K., Bourenkov, G. P., et al. (1997) · Nature · doi:10.1038/37995 · Cited by 619

Structural Evidence for Ligand Specificity in the Binding Domain of the Human Androgen Receptor

Matias, P. M., Donner, P., Coelho, R., Thomaz, M., Peixoto, C., Macedo, S., Otto, N., Joschko, S., Scholz, P., Wegg, A., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004571200 · Cited by 608

Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein

Gamble, T. R., Yoo, S., Vajdos, F. F., von Schwedler, U. K., Worthylake, D. K., Wang, H., McCutcheon, J. P., Sundquist, W. I., & Hill, C. P. (1997) · Science · doi:10.1126/science.278.5339.849 · Cited by 598

Structural basis for AMP binding to mammalian AMP-activated protein kinase

Xiao, B., Heath, R., Saiu, P., Leiper, F. C., Leone, P., Jing, C., Walker, P. A., Haire, L., Eccleston, J. F., Davis, C. T., et al. (2007) · Nature · doi:10.1038/nature06161 · Cited by 591

X-Ray Structures of Myc-Max and Mad-Max Recognizing DNA

Nair, S. K., & Burley, S. K. (2003) · Cell · doi:10.1016/s0092-8674(02)01284-9 · Cited by 551

Crystallographic structures of the ligand-binding domains of the androgen receptor and its T877A mutant complexed with the natural agonist dihydrotestosterone

Sack, J. S., Kish, K. F., Wang, C., Attar, R. M., Kiefer, S. E., An, Y., Wu, G. Y., Scheffler, J. E., Salvati, M. E., Krystek, S. R., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.081565498 · Cited by 491

The structure of the central stalk in bovine F(1)-ATPase at 2.4 A resolution.

(2000) · Nature Structural Biology · doi:10.1038/80981 · Cited by 448

Structure of Human Methionine Aminopeptidase-2 Complexed with Fumagillin

Liu, S., Widom, J., Kemp, C. W., Crews, C. M., & Clardy, J. (1998) · Science · doi:10.1126/science.282.5392.1324 · Cited by 440

The allosteric regulation of pyruvate kinase by fructose-1,6-bisphosphate

Jurica, M. S., Mesecar, A., Heath, P. J., Shi, W., Nowak, T., & Stoddard, B. L. (1998) · Structure · doi:10.1016/s0969-2126(98)00021-5 · Cited by 426

Crystal Structure at 2.8 Å of an FcRn/Heterodimeric Fc Complex

Martin, W. L., West, A. P., Gan, L., & Bjorkman, P. J. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00230-1 · Cited by 391

N- and C-Terminal Flanking Regions Modulate Light-Induced Signal Transduction in the LOV2 Domain of the Blue Light Sensor Phototropin 1 from Avena sativa ,

Halavaty, A. S., & Moffat, K. (2007) · Biochemistry · doi:10.1021/bi701543e · Cited by 317

Crystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase a receptor.

Fernandez‐Catalan, C., Bode, W., Huber, R., Turk, D., Calvete, J. J., Lichte, A., Tschesche, H., & Maskos, K. (1998) · The EMBO Journal · doi:10.1093/emboj/17.17.5238 · Cited by 321

Structural basis for recruitment of glycogen synthase kinase 3β to the axin—APC scaffold complex

Dajani, R., Fraser, E., Roe, S. M., Yeo, M., Good, V. M., Thompson, V., Dale, T. C., & Pearl, L. H. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg068 · Cited by 315

Crystal Structures of MAP Kinase p38 Complexed to the Docking Sites on Its Nuclear Substrate MEF2A and Activator MKK3b

Chang, C.-I., Xu, B.-E., Akella, R., Cobb, M. H., & Goldsmith, E. J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00525-7 · Cited by 302

Structure of Internalin, a Major Invasion Protein of Listeria monocytogenes, in Complex with Its Human Receptor E-Cadherin

Schubert, W.-D., Urbanke, C., Ziehm, T., Beier, V., Machner, M. P., Domann, E., Wehland, J., Chakraborty, T., & Heinz, D. W. (2002) · Cell · doi:10.1016/s0092-8674(02)01136-4 · Cited by 302

Comparison of Crystal Structures of Human Androgen Receptor Ligand-Binding Domain Complexed with Various Agonists Reveals Molecular Determinants Responsible for Binding Affinity

Pereira de Jésus‐Tran, K., Côté, P., Cantin, L., Blanchet, J., Labrie, F., & Breton, R. (2006) · Protein Science · doi:10.1110/ps.051905906 · Cited by 278

The structure of mitogen-activated protein kinase p38 at 2.1-Å resolution

Wang, Z., Harkins, P. C., Ulevitch, R. J., Han, J., Cobb, M. H., & Goldsmith, E. J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.6.2327 · Cited by 275

Structural Basis of Competitive Recognition of p53 and MDM2 by HAUSP/USP7: Implications for the Regulation of the p53–MDM2 Pathway

Hu, M., Gu, L., Li, M., Jeffrey, P. D., Gu, W., & Shi, Y. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040027 · Cited by 251

Munc13 C2B domain is an activity-dependent Ca2+ regulator of synaptic exocytosis

Shin, O.-H., Lu, J., Rhee, J.-S., Tomchick, D. R., Pang, Z. P., Wojcik, S. M., Camacho-Perez, M., Brose, N., Machius, M., Rizo, J., et al. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1758 · Cited by 243

Crystal structure of a β-catenin/Axin complex suggests a mechanism for the β-catenin destruction complex

Xing, Y., Clements, W. K., Kimelman, D., & Xu, W. (2003) · Genes & Development · doi:10.1101/gad.1142603 · Cited by 237

Structures of the HIV-1 capsid protein dimerization domain at 2.6 Å resolution

Worthylake, D. K., Wang, H., Yoo, S., Sundquist, W. I., & Hill, C. P. (1999) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998007689 · Cited by 235

Structural basis for recognition of AU-rich element RNA by the HuD protein.

(2001) · Nature Structural Biology · doi:10.1038/84131 · Cited by 234

All-trans retinoic acid is a ligand for the orphan nuclear receptor RORβ

Stehlin-Gaon, C., Willmann, D., Zeyer, D., Sanglier, S., Van Dorsselaer, A., Renaud, J.-P., Moras, D., & Schüle, R. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb979 · Cited by 231

Crystal structure of an IRF‐DNA complex reveals novel DNA recognition and cooperative binding to a tandem repeat of core sequences

Fujii, Y., Shimizu, T., Kusumoto, M., Kyogoku, Y., Taniguchi, T., & Hakoshima, T. (1999) · The EMBO Journal · doi:10.1093/emboj/18.18.5028 · Cited by 223

Structural Studies of Human Histone Deacetylase 8 and Its Site-Specific Variants Complexed with Substrate and Inhibitors,

Dowling, D. P., Gantt, S. L., Gattis, S. G., Fierke, C. A., & Christianson, D. W. (2008) · Biochemistry · doi:10.1021/bi801610c · Cited by 200

Crystal structure of JNK3: a kinase implicated in neuronal apoptosis

Xie, X., Gu, Y., Fox, T., Coll, J. T., Fleming, M. A., Markland, W., Caron, P. R., Wilson, K. P., & Su, M. S.-S. (1998) · Structure · doi:10.1016/s0969-2126(98)00100-2 · Cited by 198

Crystal Structure of Human RhoA in a Dominantly Active Form Complexed with a GTP Analogue

Ihara, K., Muraguchi, S., Kato, M., Shimizu, T., Shirakawa, M., Kuroda, S., Kaibuchi, K., & Hakoshima, T. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.16.9656 · Cited by 190

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

Structure of the BRCT Repeats of BRCA1 Bound to a BACH1 Phosphopeptide

Shiozaki, E. N., Gu, L., Yan, N., & Shi, Y. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00238-2 · Cited by 174

Docking Interactions Induce Exposure of Activation Loop in the MAP Kinase ERK2

Zhou, T., Sun, L., Humphreys, J., & Goldsmith, E. J. (2006) · Structure · doi:10.1016/j.str.2006.04.006 · Cited by 164

Sialic acid recognition by Vibrio cholerae neuraminidase

Moustafa, I., Connaris, H., Taylor, M., Zaitsev, V., Wilson, J. C., Kiefel, M. J., von Itzstein, M., & Taylor, G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404965200 · Cited by 165

The Role of Docking Interactions in Mediating Signaling Input, Output, and Discrimination in the Yeast MAPK Network

Reményi, A., Good, M. C., Bhattacharyya, R. P., & Lim, W. A. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.10.030 · Cited by 154

Crystal structure of PU. 1/IRF-4/DNA ternary complex

Escalante, C. R., Brass, A. L., Pongubala, J. M. R., Shatova, E., Shen, L., Singh, H., & Aggarwal, A. K. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00703-7 · Cited by 154

Structural basis of adhesion‐molecule recognition by ERM proteins revealed by the crystal structure of the radixin—ICAM‐2 complex

Hamada, K., Shimizu, T., Yonemura, S., Tsukita, S., Tsukita, S., & Hakoshima, T. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg039 · Cited by 155

Structural Basis for Catalysis and Inhibition ofN-Glycan Processing Class I α1,2-Mannosidases

Vallée, F., Karaveg, K., Herscovics, A., Moremen, K. W., & Howell, P. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006927200 · Cited by 152

Structural and redox plasticity in the heterodimeric periplasmic nitrate reductase

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

Exo84 and Sec5 are competitive regulatory Sec6/8 effectors to the RalA GTPase

Jin, R., Junutula, J. R., Matern, H. T., Ervin, K. E., Scheller, R. H., & Brunger, A. T. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600699 · Cited by 145

Structural basis of sialyltransferase activity in trypanosomal sialidases

Buschiazzo, A., Tavares, G. A., Campetella, O., Spinelli, S., Cremona, M. L., París, G., Fernanda Amaya, M., Frasch, A. C. C., & Alzari, P. M. (2000) · The EMBO Journal · doi:10.1093/emboj/19.1.16 · Cited by 138

Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity

Saul, F. A., Arié, J.-P., Vulliez-le Normand, B., Kahn, R., Betton, J.-M., & Bentley, G. A. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.10.056 · Cited by 130

The Structure of JNK3 in Complex with Small Molecule Inhibitors

Scapin, G., Patel, S. B., Lisnock, J., Becker, J. W., & LoGrasso, P. V. (2003) · Chemistry & Biology · doi:10.1016/s1074-5521(03)00159-5 · Cited by 131

Proline to arginine mutations in FGF receptors 1 and 3 result in Pfeiffer and Muenke craniosynostosis syndromes through enhancement of FGF binding affinity

Ibrahimi, O. A. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddh011 · Cited by 128

Ajoene Is an Inhibitor and Subversive Substrate of Human Glutathione Reductase and Trypanosoma cruzi Trypanothione Reductase: Crystallographic, Kinetic, and Spectroscopic Studies

Gallwitz, H., Bonse, S., Martinez-Cruz, A., Schlichting, I., Schumacher, K., & Krauth-Siegel, R. L. (1999) · Journal of Medicinal Chemistry · doi:10.1021/jm980471k · Cited by 127

Structural basis of the interaction between RalA and Sec5, a subunit of the sec6/8 complex

Fukai, S., Matern, H. T., Jagath, J. R., Scheller, R. H., & Brunger, A. T. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg329 · Cited by 126

Structure of the DNA-Bound T-Box Domain of Human TBX3, a Transcription Factor Responsible for Ulnar-Mammary Syndrome

Coll, M., Seidman, J. G., & Müller, C. W. (2002) · Structure · doi:10.1016/s0969-2126(02)00722-0 · Cited by 121

The crystal structure of the monomeric reverse transcriptase from Moloney murine leukemia virus

Das, D., & Georgiadis, M. M. (2004) · Structure · doi:10.1016/j.str.2004.02.032 · Cited by 117

Structural determinants of metal specificity in the zinc transport protein ZnuA from synechocystis 6803

Banerjee, S., Wei, B., Bhattacharyya-Pakrasi, M., Pakrasi, H. B., & Smith, T. J. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.09.008 · Cited by 113

Structure of the ternary complex of human 17β-hydroxysteroid dehydrogenase type 1 with 3-hydroxyestra-1,3,5,7-tetraen-17-one (equilin) and NADP +

Sawicki, M. W., Erman, M., Puranen, T., Vihko, P., & Ghosh, D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.3.840 · Cited by 113

The B‐box dominates SAP‐1–SRF interactions in the structure of the ternary complex

Hassler, M., & Richmond, T. J. (2001) · The EMBO Journal · doi:10.1093/emboj/20.12.3018 · Cited by 111

Molecular basis of MAPK-activated protein kinase 2:p38 assembly

White, A., Pargellis, C. A., Studts, J. M., Werneburg, B. G., & Farmer, B. T. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701679104 · Cited by 111

The crystal structure of the zymogen catalytic domain of complement protease C1r reveals that a disruptive mechanical stress is required to trigger activation of the C1 complex

Budayova‐Spano, M., Lacroix, M., Thielens, N. M., Arlaud, G. J., Fontecilla‐Camps, J. C., & Gaboriaud, C. (2002) · The EMBO Journal · doi:10.1093/emboj/21.3.231 · Cited by 111

Activation of Human Liver Glycogen Phosphorylase by Alteration of the Secondary Structure and Packing of the Catalytic Core

Rath, V. L., Ammirati, M., LeMotte, P. K., Fennell, K. F., Mansour, M. N., Danley, D. E., Hynes, T. R., Schulte, G. K., Wasilko, D. J., & Pandit, J. (2000) · Molecular Cell · doi:10.1016/s1097-2765(05)00006-7 · Cited by 107

Structures of SAP-1 Bound to DNA Targets from the E74 and c-fos Promoters

Mo, Y., Vaessen, B., Johnston, K., & Marmorstein, R. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80130-6 · Cited by 103

Crystal structure of a ternary SAP-1/SRF/ c-fos SRE DNA complex 1 1Edited by K. Morikawa

Mo, Y., Ho, W., Johnston, K., & Marmorstein, R. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5138 · Cited by 78

Crystal structure of isopentenyl diphosphate:dimethylallyl diphosphate isomerase

Durbecq, V., Sainz, G., Oudjama, Y., Clantin, B., Bompard‐Gilles, C., Tricot, C., Caillet, J., Stalon, V., Droogmans, L., & Villeret, V. (2001) · The EMBO Journal · doi:10.1093/emboj/20.7.1530 · Cited by 90

Crystal Structure of the Catalytic Domain of Human ADAM33

Orth, P., Reichert, P., Wang, W., Prosise, W. W., Yarosh-Tomaine, T., Hammond, G., Ingram, R. N., Xiao, L., Mirza, U. A., Zou, J., et al. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.10.037 · Cited by 90

Structure and reactivity of LpxD, the N -acyltransferase of lipid A biosynthesis

Buetow, L., Smith, T. K., Dawson, A., Fyffe, S., & Hunter, W. N. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606356104 · Cited by 78

Structural Basis for Phosphotyrosine Recognition by Suppressor of Cytokine Signaling-3

Bergamin, E., Wu, J., & Hubbard, S. R. (2006) · Structure · doi:10.1016/j.str.2006.06.011 · Cited by 60

Dimeric Rous Sarcoma Virus Capsid Protein Structure Relevant to Immature Gag Assembly

Nandhagopal, N., Simpson, A. A., Johnson, M. C., Francisco, A. B., Schatz, G. W., Rossmann, M. G., & Vogt, V. M. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.10.034 · Cited by 44

Crystal structure of the catalytic domain of MMP-16/MT3-MMP: Characterization of MT-MMP specific features.

Lang, R., Braun, M., Sounni, N. E., Noel, A., Frankenne, F., Foidart, J.-M., Bode, W., & Maskos, K. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.12.022 · Cited by 42

Structure of the N-terminal domain of human FKBP52

Li, P., Ding, Y., Wu, B., Shu, C., Shen, B., & Rao, Z. (2003) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444902017523 · Cited by 32

Structure of the manganese superoxide dismutase from Deinococcus radiodurans in two crystal forms

Dennis, R. J., Micossi, E., McCarthy, J., Moe, E., Gordon, E. J., Kozielski-Stuhrmann, S., Leonard, G. A., & McSweeney, S. (2006) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309106008402 · Cited by 30

Structure of the putative DNA-binding protein SP_1288 from Streptococcus pyogenes

Oganesyan, V., Pufan, R., DeGiovanni, A., Yokota, H., Kim, R., & Kim, S.-H. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904009394 · Cited by 9

Allosteric Regulation in the Ligand Binding Domain of Retinoic Acid Receptorγ

Chebaro, Y., Sirigu, S., Amal, I., Lutzing, R., Stote, R. H., Rochette-Egly, C., Rochel, N., & Dejaegere, A. (2017) · PLOS ONE · doi:10.1371/journal.pone.0171043 · Cited by 8

Untitled work

(1999) · doi:10.1002/(sici)1097-0134(1999)37:3+<171::aid-prot21>3.0.co;2-z