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Marcia, M., and Pyle, A. Marie (2012) Visualizing group II intron catalysis through the stages of splicing. Cell. 151, 497-507
Manigrasso, J., Chillón, I., Genna, V., Vidossich, P., Somarowthu, S., Pyle, A. Marie, De Vivo, M., and Marcia, M. (2020) Visualizing group II intron dynamics between the first and second steps of splicing. Nat Commun. 11, 2837
Kung, Y., Ando, N., Doukov, T. I., Blasiak, L. C., Bender, G., Seravalli, J., Ragsdale, S. W., and Drennan, C. L. (2012) Visualizing molecular juggling within a B12-dependent methyltransferase complex. Nature. 484, 265-9
Hirschi, M., Johnson, Z. Lee, and Lee, S. - Y. (2017) Visualizing multistep elevator-like transitions of a nucleoside transporter. Nature. 545, 66-70
Luo, D., Kohlway, A., Vela, A., and Pyle, A. Marie (2012) Visualizing the determinants of viral RNA recognition by innate immune sensor RIG-I. Structure. 20, 1983-8
Biester, A., Dementin, S., and Drennan, C. L. (2022) Visualizing the gas channel of a monofunctional carbon monoxide dehydrogenase. J Inorg Biochem. 230, 111774
Kumar, N., Leonzino, M., Hancock-Cerutti, W., Horenkamp, F. A., Li, P. Q., Lees, J. A., Wheeler, H., Reinisch, K. M., and De Camilli, P. (2018) VPS13A and VPS13C are lipid transport proteins differentially localized at ER contact sites. J Cell Biol. 217, 3625-3639
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Shen, G., Cui, W., Zhang, H., Zhou, F., Huang, W., Liu, Q., Yang, Y., Li, S., Bowman, G. R., J Sadler, E., Gross, M. L., and Li, W. (2017) Warfarin traps human vitamin K epoxide reductase in an intermediate state during electron transfer. Nat Struct Mol Biol. 24, 69-76
Li, K., Yatsunyk, L., and Neidle, S. (2021) Water spines and networks in G-quadruplex structures. Nucleic Acids Res. 49, 519-528
Schirle, N. T., Sheu-Gruttadauria, J., Chandradoss, S. D., Joo, C., and MacRae, I. J. (2015) Water-mediated recognition of t1-adenosine anchors Argonaute2 to microRNA targets. Elife. 10.7554/eLife.07646
Smiley, A. T., Tompkins, K. J., Pawlak, M. R., Krueger, A. J., Evans, R. L., Shi, K., Aihara, H., and Gordon, W. R. (2022) Watson-Crick Base-Pairing Requirements for ssDNA Recognition and Processing in Replication-Initiating HUH Endonucleases. mBio. 10.1128/mbio.02587-22
Luo, Z., Rajashankar, K., and Dauter, Z. (2014) Weak data do not make a free lunch, only a cheap meal. Acta Crystallogr D Biol Crystallogr. 70, 253-60
Ginn, J., Jiang, X., Sun, S., Michino, M., Huggins, D. J., Mbambo, Z., Jansen, R., Rhee, K. Y., Arango, N., Lima, C. D., Liverton, N., Imaeda, T., Okamoto, R., Kuroita, T., Aso, K., Stamford, A., Foley, M., Meinke, P. T., Nathan, C., and Bryk, R. (2021) Whole Cell Active Inhibitors of Mycobacterial Lipoamide Dehydrogenase Afford Selectivity over the Human Enzyme through Tight Binding Interactions. ACS Infect Dis. 7, 435-444
Rugel, A. R., Guzman, M. A., Taylor, A. B., Chevalier, F. D., Tarpley, R. S., McHardy, S. F., Cao, X., Holloway, S. P., Anderson, T. J. C., P Hart, J., and LoVerde, P. T. (2020) Why does oxamniquine kill Schistosoma mansoni and not S. haematobium and S. japonicum?. Int J Parasitol Drugs Drug Resist. 13, 8-15
Rizzolo, K., Cohen, S. E., Weitz, A. C., Muñoz, M. M. López, Hendrich, M. P., Drennan, C. L., and Elliott, S. J. (2019) A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state. Nat Commun. 10, 1101
Bradshaw, N., Levdikov, V. M., Zimanyi, C. M., Gaudet, R., Wilkinson, A. J., and Losick, R. (2017) A widespread family of serine/threonine protein phosphatases shares a common regulatory switch with proteasomal proteases. Elife. 10.7554/eLife.26111
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Goldman, P. J., Grove, T. L., Booker, S. J., and Drennan, C. L. (2013) X-ray analysis of butirosin biosynthetic enzyme BtrN redefines structural motifs for AdoMet radical chemistry. Proc Natl Acad Sci U S A. 110, 15949-54
Fan, C., Fan, M., Orlando, B. J., Fastman, N. M., Zhang, J., Xu, Y., Chambers, M. G., Xu, X., Perry, K., Liao, M., and Feng, L. (2018) X-ray and cryo-EM structures of the mitochondrial calcium uniporter. Nature. 559, 575-579
Agdanowski, M. P., Castells-Graells, R., Sawaya, M. R., Cascio, D., Yeates, T. O., and Arbing, M. A. (2024) X-ray crystal structure of a designed rigidified imaging scaffold in the ligand-free conformation. Acta Crystallogr F Struct Biol Commun. 80, 107-115
Han, S., Le, B. V., Hajare, H. S., Baxter, R. H. G., and Miller, S. J. (2014) X-ray crystal structure of teicoplanin A₂-2 bound to a catalytic peptide sequence via the carrier protein strategy.. J Org Chem. 79, 8550-6
Jones, J. C., Banerjee, R., Semonis, M. M., Shi, K., Aihara, H., and Lipscomb, J. D. (2022) X-ray Crystal Structures of Methane Monooxygenase Hydroxylase Complexes with Variants of Its Regulatory Component: Correlations with Altered Reaction Cycle Dynamics. Biochemistry. 61, 21-33
Caldwell, J. T., Mermelstein, D. J., Walker, R. C., Bernstein, S. I., and Huxford, T. (2019) X-ray crystallographic and molecular dynamic analyses of Drosophila melanogaster embryonic muscle myosin define domains responsible for isoform-specific properties. J Mol Biol. 10.1016/j.jmb.2019.11.013
Wada, M., Heux, L., Nishiyama, Y., and Langan, P. (2009) X-ray crystallographic, scanning microprobe X-ray diffraction, and cross-polarized/magic angle spinning 13C NMR studies of the structure of cellulose III(II). Biomacromolecules. 10, 302-9
Herbst-Gervasoni, C. J., and Christianson, D. W. (2021) X-ray Crystallographic Snapshots of Substrate Binding in the Active Site of Histone Deacetylase 10. Biochemistry. 10.1021/acs.biochem.0c00936
Zhu, N., Mealka, M., Mitchel, S., Milani, C., Acuña, L. M., Rogers, E., Lahana, A. N., and Huxford, T. (2023) X-ray Crystallographic Study of Preferred Spacing by the NF-κB p50 Homodimer on κB DNA.. Biomolecules. 10.3390/biom13091310

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