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Köksal, M., Hu, H., Coates, R. M., Peters, R. J., and Christianson, D. W. (2011) Structure and mechanism of the diterpene cyclase ent-copalyl diphosphate synthase. Nat Chem Biol. 7, 431-3

Kattke, M. D., Gosschalk, J. E., Martinez, O. E., Kumar, G., Gale, R. T., Cascio, D., Sawaya, M. R., Philips, M., Brown, E. D., and Clubb, R. T. (2019) Structure and mechanism of TagA, a novel membrane-associated glycosyltransferase that produces wall teichoic acids in pathogenic bacteria. PLoS Pathog. 15, e1007723

Kattke, M. D., Gosschalk, J. E., Martinez, O. E., Kumar, G., Gale, R. T., Cascio, D., Sawaya, M. R., Philips, M., Brown, E. D., and Clubb, R. T. (2019) Structure and mechanism of TagA, a novel membrane-associated glycosyltransferase that produces wall teichoic acids in pathogenic bacteria. PLoS Pathog. 15, e1007723

Siegel, S. D., Amer, B. R., Wu, C., Sawaya, M. R., Gosschalk, J. E., Clubb, R. T., and Ton-That, H. (2019) Structure and Mechanism of LcpA, a Phosphotransferase That Mediates Glycosylation of a Gram-Positive Bacterial Cell Wall-Anchored Protein. MBio. 10.1128/mBio.01580-18

Park, E., Kim, N., Ficarro, S. B., Zhang, Y., Lee, B. Il, Cho, A., Kim, K., Park, A. K. J., Park, W. - Y., Murray, B., Meyerson, M., Beroukhim, R., Marto, J. A., Cho, J., and Eck, M. J. (2015) Structure and mechanism of activity-based inhibition of the EGF receptor by Mig6. Nat Struct Mol Biol. 22, 703-711

Park, E., Kim, N., Ficarro, S. B., Zhang, Y., Lee, B. Il, Cho, A., Kim, K., Park, A. K. J., Park, W. - Y., Murray, B., Meyerson, M., Beroukhim, R., Marto, J. A., Cho, J., and Eck, M. J. (2015) Structure and mechanism of activity-based inhibition of the EGF receptor by Mig6. Nat Struct Mol Biol. 22, 703-711

Sanches, M., Duffy, N. M., Talukdar, M., Thevakumaran, N., Chiovitti, D., Canny, M. D., Lee, K., Kurinov, I., Uehling, D., Al-awar, R., Poda, G., Prakesch, M., Wilson, B., Tam, V., Schweitzer, C., Toro, A., Lucas, J. L., Vuga, D., Lehmann, L., Durocher, D., Zeng, Q., Patterson, J. B., and Sicheri, F. (2014) Structure and mechanism of action of the hydroxy-aryl-aldehyde class of IRE1 endoribonuclease inhibitors. Nat Commun. 5, 4202

Sanches, M., Duffy, N. M., Talukdar, M., Thevakumaran, N., Chiovitti, D., Canny, M. D., Lee, K., Kurinov, I., Uehling, D., Al-awar, R., Poda, G., Prakesch, M., Wilson, B., Tam, V., Schweitzer, C., Toro, A., Lucas, J. L., Vuga, D., Lehmann, L., Durocher, D., Zeng, Q., Patterson, J. B., and Sicheri, F. (2014) Structure and mechanism of action of the hydroxy-aryl-aldehyde class of IRE1 endoribonuclease inhibitors. Nat Commun. 5, 4202

Lau, R. K., Ye, Q., Birkholz, E. A., Berg, K. R., Patel, L., Mathews, I. T., Watrous, J. D., Ego, K., Whiteley, A. T., Lowey, B., Mekalanos, J. J., Kranzusch, P. J., Jain, M., Pogliano, J., and Corbett, K. D. (2020) Structure and Mechanism of a Cyclic Trinucleotide-Activated Bacterial Endonuclease Mediating Bacteriophage Immunity. Mol Cell. 10.1016/j.molcel.2019.12.010

Singh, M., Wang, Z., Cascio, D., and Feigon, J. (2015) Structure and interactions of the CS domain of human H/ACA RNP assembly protein Shq1. J Mol Biol. 427, 807-23

Wheatley, N. M., Sundberg, C. D., Gidaniyan, S. D., Cascio, D., and Yeates, T. O. (2014) Structure and identification of a pterin dehydratase-like protein as a ribulose-bisphosphate carboxylase/oxygenase (RuBisCO) assembly factor in the α-carboxysome.. J Biol Chem. 289, 7973-81

Singh, M., Gonzales, F. A., Cascio, D., Heckmann, N., Chanfreau, G., and Feigon, J. (2009) Structure and functional studies of the CS domain of the essential H/ACA ribonucleoparticle assembly protein SHQ1. J Biol Chem. 284, 1906-16

Singh, M., Gonzales, F. A., Cascio, D., Heckmann, N., Chanfreau, G., and Feigon, J. (2009) Structure and functional studies of the CS domain of the essential H/ACA ribonucleoparticle assembly protein SHQ1. J Biol Chem. 284, 1906-16

Trachman, R. J., Autour, A., C Y Jeng, S., Abdolahzadeh, A., Andreoni, A., Cojocaru, R., Garipov, R., Dolgosheina, E. V., Knutson, J. R., Ryckelynck, M., Unrau, P. J., and Ferré-D'Amaré, A. R. (2019) Structure and functional reselection of the Mango-III fluorogenic RNA aptamer. Nat Chem Biol. 15, 472-479

Trachman, R. J., Autour, A., C Y Jeng, S., Abdolahzadeh, A., Andreoni, A., Cojocaru, R., Garipov, R., Dolgosheina, E. V., Knutson, J. R., Ryckelynck, M., Unrau, P. J., and Ferré-D'Amaré, A. R. (2019) Structure and functional reselection of the Mango-III fluorogenic RNA aptamer. Nat Chem Biol. 15, 472-479

Geng, Y., Xiong, D., Mosyak, L., Malito, D. L., Kniazeff, J., Chen, Y., Burmakina, S., Quick, M., Bush, M., Javitch, J. A., Pin, J. - P., and Fan, Q. R. (2012) Structure and functional interaction of the extracellular domain of human GABA(B) receptor GBR2. Nat Neurosci. 15, 970-8

Doamekpor, S. K., Lee, J. - W., Hepowit, N. L., Wu, C., Charenton, C., Leonard, M., Bengtson, M. H., Rajashankar, K. R., Sachs, M. S., Lima, C. D., and Joazeiro, C. A. P. (2016) Structure and function of the yeast listerin (Ltn1) conserved N-terminal domain in binding to stalled 60S ribosomal subunits. Proc Natl Acad Sci U S A. 113, E4151-60

Hubin, E. A., Fay, A., Xu, C., Bean, J. M., Saecker, R. M., Glickman, M. S., Darst, S. A., and Campbell, E. A. (2017) Structure and function of the mycobacterial transcription initiation complex with the essential regulator RbpA. Elife. 10.7554/eLife.22520

Zheng, J., Sagar, V., Smolinsky, A., Bourke, C., LaRonde-LeBlanc, N., and T Cropp, A. (2009) Structure and function of the macrolide biosensor protein, MphR(A), with and without erythromycin. J Mol Biol. 387, 1250-60

Osko, J. D., Roose, B. W., Shinsky, S. A., and Christianson, D. W. (2019) Structure and Function of the Acetylpolyamine Amidohydrolase from the Deep Earth Halophile . Biochemistry. 58, 3755-3766

Su, C. - C., Bolla, J. Reddy, Kumar, N., Radhakrishnan, A., Long, F., Delmar, J. A., Chou, T. - H., Rajashankar, K. R., Shafer, W. M., and Yu, E. W. (2015) Structure and function of Neisseria gonorrhoeae MtrF illuminates a class of antimetabolite efflux pumps. Cell Rep. 11, 61-70

Kono, A., Chou, T. - H., Radhakrishnan, A., Bolla, J. Reddy, Sankar, K., Shome, S., Su, C. - C., Jernigan, R. L., Robinson, C. V., Yu, E. W., and Spalding, M. H. (2020) Structure and Function of LCI1: A plasma membrane CO channel in the Chlamydomonas CO concentrating mechanism. Plant J. 10.1111/tpj.14745

Chen, M., Chou, W. K. W., Toyomasu, T., Cane, D. E., and Christianson, D. W. (2016) Structure and Function of Fusicoccadiene Synthase, a Hexameric Bifunctional Diterpene Synthase. ACS Chem Biol. 11, 889-99

Chen, M., Chou, W. K. W., Toyomasu, T., Cane, D. E., and Christianson, D. W. (2016) Structure and Function of Fusicoccadiene Synthase, a Hexameric Bifunctional Diterpene Synthase. ACS Chem Biol. 11, 889-99

Chen, M., Chou, W. K. W., Toyomasu, T., Cane, D. E., and Christianson, D. W. (2016) Structure and Function of Fusicoccadiene Synthase, a Hexameric Bifunctional Diterpene Synthase. ACS Chem Biol. 11, 889-99

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The Northeastern Collaborative Access Team (NE-CAT) facility at the Advanced Photon Source at Argonne National Laboratory is managed by Cornell University and consists of seven member institutions:

Columbia University
Cornell University
Harvard University
Memorial Sloan-Kettering Cancer Center
Massachusetts Institute of Technology
Rockefeller University
Yale University

Primary funding for this project comes from the National Institute of General Medical Sciences (NIGMS), a division of the National Institutes of Health (NIH). Additional financial support for NE-CAT comes from the member institutions.