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Geldenhuys, W. J., Long, T. E., Saralkar, P., Iwasaki, T., Nuñez, R. A. A., Nair, R. R., Konkle, M. E., Menze, M. A., Pinti, M. V., Hollander, J. M., Hazlehurst, L. A., and Robart, A. R. (2019) Crystal structure of the mitochondrial protein mitoNEET bound to a benze-sulfonide ligand. Communications Chemistry. 2, 77
Semavina, M., Saha, N., Kolev, M. V., Goldgur, Y., Giger, R. J., Himanen, J. P., and Nikolov, D. B. (2011) Crystal structure of the Nogo-receptor-2. Protein Sci. 20, 684-9
Xu, K., Chan, Y. - P., Bradel-Tretheway, B., Akyol-Ataman, Z., Zhu, Y., Dutta, S., Yan, L., Feng, Y. R., Wang, L. - F., Skiniotis, G., Lee, B., Z Zhou, H., Broder, C. C., Aguilar, H. C., and Nikolov, D. B. (2015) Crystal Structure of the Pre-fusion Nipah Virus Fusion Glycoprotein Reveals a Novel Hexamer-of-Trimers Assembly. PLoS Pathog. 11, e1005322
Everett, B. A., Litzau, L. A., Tompkins, K., Shi, K., Nelson, A., Aihara, H., Iii, R. L. Evans, and Gordon, W. R. (2019) Crystal structure of the Wheat dwarf virus Rep domain. Acta Crystallogr F Struct Biol Commun. 75, 744-749
Dhatwalia, R., Singh, H., Oppenheimer, M., Karr, D. B., Nix, J. C., Sobrado, P., and Tanner, J. J. (2012) Crystal structures and small-angle x-ray scattering analysis of UDP-galactopyranose mutase from the pathogenic fungus Aspergillus fumigatus. J Biol Chem. 287, 9041-51
Feliciano, P. R., Drennan, C. L., and Nonato, M. Cristina (2019) Crystal structures of fumarate hydratases from Leishmania major in a complex with inhibitor 2-thiomalate. ACS Chem Biol. 10.1021/acschembio.8b00972
Xu, K., Xu, Y., Rajashankar, K. R., Robev, D., and Nikolov, D. B. (2013) Crystal structures of Lgr4 and its complex with R-spondin1. Structure. 21, 1683-9
Gao, L., Lam, K. - H., Liu, S., Przykopanski, A., Lübke, J., Qi, R., Krüger, M., Nowakowska, M. B., Selby, K., Douillard, F. P., Dorner, M. B., Perry, K., Lindström, M., Dorner, B. G., Rummel, A., and Jin, R. (2023) Crystal structures of OrfX1, OrfX2 and the OrfX1-OrfX3 complex from the orfX gene cluster of botulinum neurotoxin E1. FEBS Lett. 597, 524-537
Barton, W. A., Tzvetkova-Robev, D., Miranda, E. P., Kolev, M. V., Rajashankar, K. R., Himanen, J. P., and Nikolov, D. B. (2006) Crystal structures of the Tie2 receptor ectodomain and the angiopoietin-2-Tie2 complex. Nat Struct Mol Biol. 13, 524-32
Yuan, L., Gao, F., Lv, Z., Nayak, D., Nayak, A., Bury, P. Dos Santos, Cano, K. E., Jia, L., Oleinik, N., Atilgan, F. Cansu, Ogretmen, B., Williams, K. M., Davies, C., Oualid, F. El, Wasmuth, E. V., and Olsen, S. K. (2022) Crystal structures reveal catalytic and regulatory mechanisms of the dual-specificity ubiquitin/FAT10 E1 enzyme Uba6. Nat Commun. 13, 4880
Yuan, L., Gao, F., Lv, Z., Nayak, D., Nayak, A., Bury, P. Dos Santos, Cano, K. E., Jia, L., Oleinik, N., Atilgan, F. Cansu, Ogretmen, B., Williams, K. M., Davies, C., Oualid, F. El, Wasmuth, E. V., and Olsen, S. K. (2022) Crystal structures reveal catalytic and regulatory mechanisms of the dual-specificity ubiquitin/FAT10 E1 enzyme Uba6. Nat Commun. 13, 4880
Sartmatova, D., Nash, T., Schormann, N., Nuth, M., Ricciardi, R., Banerjee, S., and Chattopadhyay, D. (2013) Crystallization and preliminary X-ray diffraction analysis of three recombinant mutants of Vaccinia virus uracil DNA glycosylase. Acta Crystallogr Sect F Struct Biol Cryst Commun. 69, 295-301
Sartmatova, D., Nash, T., Schormann, N., Nuth, M., Ricciardi, R., Banerjee, S., and Chattopadhyay, D. (2013) Crystallization and preliminary X-ray diffraction analysis of three recombinant mutants of Vaccinia virus uracil DNA glycosylase. Acta Crystallogr Sect F Struct Biol Cryst Commun. 69, 295-301
Young, T., Niks, D., Hakopian, S., Tam, T. K., Yu, X., Hille, R., and Blaha, G. M. (2020) Crystallographic and kinetic analyses of the FdsBG subcomplex of the cytosolic formate dehydrogenase FdsABG from Cupriavidus necator. J Biol Chem. 10.1074/jbc.RA120.013264
Wang, Y., Sosinowski, T., Novikov, A., Crawford, F., Neau, D. B., Yang, J., Kwok, W. W., Marrack, P., Kappler, J. W., and Dai, S. (2018) C-terminal modification of the insulin B:11-23 peptide creates superagonists in mouse and human type 1 diabetes. Proc Natl Acad Sci U S A. 115, 162-167
Wang, Y., Sosinowski, T., Novikov, A., Crawford, F., Neau, D. B., Yang, J., Kwok, W. W., Marrack, P., Kappler, J. W., and Dai, S. (2018) C-terminal modification of the insulin B:11-23 peptide creates superagonists in mouse and human type 1 diabetes. Proc Natl Acad Sci U S A. 115, 162-167
D
Murphy, F., Schuermann, J., Neau, D., Perry, K., and Rajashankar, K. R. (2019) Data Analysis in Real Time with RAPDv2.0. 2019 Annual Meeting of the American Crystallographic Association, July 20-24, 2019
Meyer, P. A., Socias, S., Key, J., Ransey, E., Tjon, E. C., Buschiazzo, A., Lei, M., Botka, C., Withrow, J., Neau, D., Rajashankar, K., Anderson, K. S., Baxter, R. H., Blacklow, S. C., Boggon, T. J., Bonvin, A. M. J. J., Borek, D., Brett, T. J., Caflisch, A., Chang, C. - I., Chazin, W. J., Corbett, K. D., Cosgrove, M. S., Crosson, S., Dhe-Paganon, S., Di Cera, E., Drennan, C. L., Eck, M. J., Eichman, B. F., Fan, Q. R., Ferré-D'Amaré, A. R., J Fromme, C., K Garcia, C., Gaudet, R., Gong, P., Harrison, S. C., Heldwein, E. E., Jia, Z., Keenan, R. J., Kruse, A. C., Kvansakul, M., McLellan, J. S., Modis, Y., Nam, Y., Otwinowski, Z., Pai, E. F., Pereira, P. José Barb, Petosa, C., Raman, C. S., Rapoport, T. A., Roll-Mecak, A., Rosen, M. K., Rudenko, G., Schlessinger, J., Schwartz, T. U., Shamoo, Y., Sondermann, H., Tao, Y. J., Tolia, N. H., Tsodikov, O. V., Westover, K. D., Wu, H., Foster, I., Fraser, J. S., Maia, F. R. N. C., Gonen, T., Kirchhausen, T., Diederichs, K., Crosas, M., and Sliz, P. (2016) Data publication with the structural biology data grid supports live analysis. Nat Commun. 7, 10882
Meyer, P. A., Socias, S., Key, J., Ransey, E., Tjon, E. C., Buschiazzo, A., Lei, M., Botka, C., Withrow, J., Neau, D., Rajashankar, K., Anderson, K. S., Baxter, R. H., Blacklow, S. C., Boggon, T. J., Bonvin, A. M. J. J., Borek, D., Brett, T. J., Caflisch, A., Chang, C. - I., Chazin, W. J., Corbett, K. D., Cosgrove, M. S., Crosson, S., Dhe-Paganon, S., Di Cera, E., Drennan, C. L., Eck, M. J., Eichman, B. F., Fan, Q. R., Ferré-D'Amaré, A. R., J Fromme, C., K Garcia, C., Gaudet, R., Gong, P., Harrison, S. C., Heldwein, E. E., Jia, Z., Keenan, R. J., Kruse, A. C., Kvansakul, M., McLellan, J. S., Modis, Y., Nam, Y., Otwinowski, Z., Pai, E. F., Pereira, P. José Barb, Petosa, C., Raman, C. S., Rapoport, T. A., Roll-Mecak, A., Rosen, M. K., Rudenko, G., Schlessinger, J., Schwartz, T. U., Shamoo, Y., Sondermann, H., Tao, Y. J., Tolia, N. H., Tsodikov, O. V., Westover, K. D., Wu, H., Foster, I., Fraser, J. S., Maia, F. R. N. C., Gonen, T., Kirchhausen, T., Diederichs, K., Crosas, M., and Sliz, P. (2016) Data publication with the structural biology data grid supports live analysis. Nat Commun. 7, 10882
Kim, D. E., Jensen, D. R., Feldman, D., Tischer, D., Saleem, A., Chow, C. M., Li, X., Carter, L., Milles, L., Nguyen, H., Kang, A., Bera, A. K., Peterson, F. C., Volkman, B. F., Ovchinnikov, S., and Baker, D. (2023) De novo design of small beta barrel proteins. Proc Natl Acad Sci U S A. 120, e2207974120
de Haas, R. J., Tas, R. P., van den Broek, D., Zheng, C., Nguyen, H., Kang, A., Bera, A. K., King, N. P., Voets, I. K., and de Vries, R. (2023) De novo designed ice-binding proteins from twist-constrained helices. Proc Natl Acad Sci U S A. 120, e2220380120
Anishchenko, I., Pellock, S. J., Chidyausiku, T. M., Ramelot, T. A., Ovchinnikov, S., Hao, J., Bafna, K., Norn, C., Kang, A., Bera, A. K., DiMaio, F., Carter, L., Chow, C. M., Montelione, G. T., and Baker, D. (2021) De novo protein design by deep network hallucination. Nature. 10.1038/s41586-021-04184-w
Zhan, C., Patskovsky, Y., Yan, Q., Li, Z., Ramagopal, U., Cheng, H., Brenowitz, M., Hui, X., Nathenson, S. G., and Almo, S. C. (2011) Decoy strategies: the structure of TL1A:DcR3 complex. Structure. 19, 162-71
Ketcham, J. M., Haling, J., Khare, S., Bowcut, V., Briere, D. M., Burns, A. C., Gunn, R. J., Ivetac, A., Kuehler, J., Kulyk, S., Laguer, J., J Lawson, D., Moya, K., Nguyen, N., Rahbaek, L., Saechao, B., Smith, C. R., Sudhakar, N., Thomas, N. C., Vegar, L., Vanderpool, D., Wang, X., Yan, L., Olson, P., Christensen, J. G., and Marx, M. A. (2022) Design and Discovery of MRTX0902, a Potent, Selective, Brain-Penetrant, and Orally Bioavailable Inhibitor of the SOS1:KRAS Protein-Protein Interaction. J Med Chem. 65, 9678-9690
Cannon, K. A., Park, R. U., Boyken, S. E., Nattermann, U., Yi, S., Baker, D., King, N. P., and Yeates, T. O. (2019) Design and structure of two new protein cages illustrate successes and ongoing challenges in protein engineering. Protein Sci. 10.1002/pro.3802

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