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A
Ausin, I., Greenberg, M. V. C., Simanshu, D. K., Hale, C. J., Vashisht, A. A., Simon, S. A., Lee, T. -fen, Feng, S., Española, S. D., Meyers, B. C., Wohlschlegel, J. A., Patel, D. J., and Jacobsen, S. E. (2012) INVOLVED IN DE NOVO 2-containing complex involved in RNA-directed DNA methylation in Arabidopsis. Proc Natl Acad Sci U S A. 109, 8374-81
Avital-Shmilovici, M., Mandal, K., Gates, Z. P., Phillips, N. B., Weiss, M. A., and Kent, S. B. H. (2013) Fully convergent chemical synthesis of ester insulin: determination of the high resolution X-ray structure by racemic protein crystallography. J Am Chem Soc. 135, 3173-85
Ayres, C. A., Schormann, N., Senkovich, O., Fry, A., Banerjee, S., Ulett, G. C., and Chattopadhyay, D. (2014) Structure of Streptococcus agalactiae glyceraldehyde-3-phosphate dehydrogenase holoenzyme reveals a novel surface. Acta Crystallogr F Struct Biol Commun. 70, 1333-9
B
Babault, N., Allali-Hassani, A., Li, F., Fan, J., Yue, A., Ju, K., Liu, F., Vedadi, M., Liu, J., and Jin, J. (2018) Discovery of Bisubstrate Inhibitors of Nicotinamide N-Methyltransferase (NNMT). J Med Chem. 61, 1541-1551
Babayeva, N. D., Wilder, P. J., Shiina, M., Mino, K., Desler, M., Ogata, K., Rizzino, A., and Tahirov, T. H. (2010) Structural basis of Ets1 cooperative binding to palindromic sequences on stromelysin-1 promoter DNA. Cell Cycle. 9, 3054-62
Babayeva, N. D., Baranovskaya, O. I., and Tahirov, T. H. (2012) Structural basis of Ets1 cooperative binding to widely separated sites on promoter DNA. PLoS One. 7, e33698
Bacik, J. - P., Walker, J. R., Ali, M., Schimmer, A. D., and Dhe-Paganon, S. (2010) Crystal structure of the human ubiquitin-activating enzyme 5 (UBA5) bound to ATP: mechanistic insights into a minimalistic E1 enzyme. J Biol Chem. 285, 20273-80
Backman, L. Rf, Huang, Y. Y., Andorfer, M. C., Gold, B., Raines, R. T., Balskus, E. P., and Drennan, C. L. (2020) Molecular basis for catabolism of the abundant metabolite -4-hydroxy-L-proline by a microbial glycyl radical enzyme. Elife. 10.7554/eLife.51420
Baconguis, I., and Gouaux, E. (2012) Structural plasticity and dynamic selectivity of acid-sensing ion channel-spider toxin complexes. Nature. 489, 400-5
Bae, B., Davis, E., Brown, D., Campbell, E. A., Wigneshweraraj, S., and Darst, S. A. (2013) Phage T7 Gp2 inhibition of Escherichia coli RNA polymerase involves misappropriation of σ70 domain 1.1.. Proc Natl Acad Sci U S A. 110, 19772-7
Bae, B., Feklistov, A., Lass-Napiorkowska, A., Landick, R., and Darst, S. A. (2015) Structure of a bacterial RNA polymerase holoenzyme open promoter complex. Elife. 10.7554/eLife.08504
Bae, H., Viennet, T., Park, E., Chu, N., Salguero, A., Eck, M. J., Arthanari, H., and Cole, P. A. (2022) PH domain-mediated autoinhibition and oncogenic activation of Akt. Elife. 10.7554/eLife.80148
Bai, Y., McCoy, J. G., Levin, E. J., Sobrado, P., Rajashankar, K. R., Fox, B. G., and Zhou, M. (2015) X-ray structure of a mammalian stearoyl-CoA desaturase. Nature. 524, 252-6
Baidin, V., Owens, T. W., Lazarus, M. B., and Kahne, D. (2021) Simple Secondary Amines Inhibit Growth of Gram-Negative Bacteria through Highly Selective Binding to Phenylalanyl-tRNA Synthetase. J Am Chem Soc. 143, 623-627
Bailey, S., Wing, R. A., and Steitz, T. A. (2006) The structure of T. aquaticus DNA polymerase III is distinct from eukaryotic replicative DNA polymerases. Cell. 126, 893-904
Bailey, S., Eliason, W. K., and Steitz, T. A. (2007) Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase. Science. 318, 459-63
Bailey, L. J., Sheehy, K. M., Dominik, P. K., Liang, W. G., Rui, H., Clark, M., Jaskolowski, M., Kim, Y., Deneka, D., Tang, W. - J., and Kossiakoff, A. A. (2018) Locking the Elbow: Improved Antibody Fab Fragments as Chaperones for Structure Determination. J Mol Biol. 430, 337-347
R Bajaj, A., Arbing, M. A., Shin, A., Cascio, D., and Miallau, L. (2016) Crystal structure of the toxin Msmeg_6760, the structural homolog of Mycobacterium tuberculosis Rv2035, a novel type II toxin involved in the hypoxic response. Acta Crystallogr F Struct Biol Commun. 72, 863-869
Bajic, G., and Harrison, S. C. (2020) Antibodies That Engage the Hemagglutinin Receptor-Binding Site of Influenza B Viruses. ACS Infect Dis. 10.1021/acsinfecdis.0c00726
Bajic, G., Maron, M. J., Adachi, Y., Onodera, T., McCarthy, K. R., McGee, C. E., Sempowski, G. D., Takahashi, Y., Kelsoe, G., Kuraoka, M., and Schmidt, A. G. (2019) Influenza Antigen Engineering Focuses Immune Responses to a Subdominant but Broadly Protective Viral Epitope. Cell Host Microbe. 25, 827-835.e6
Baker, B. Y., Shi, W., Wang, B., and Palczewski, K. (2014) High-resolution crystal structures of the photoreceptor glyceraldehyde 3-phosphate dehydrogenase (GAPDH) with three and four-bound NAD molecules. Protein Sci. 23, 1629-39
Baker, B. Y., Gulati, S., Shi, W., Wang, B., Stewart, P. L., and Palczewski, K. (2015) Crystallization of proteins from crude bovine rod outer segments. Methods Enzymol. 557, 439-58
Balaratnam, S., Torrey, Z. R., Calabrese, D. R., Banco, M. T., Yazdani, K., Liang, X., Fullenkamp, C. R., Seshadri, S., Holewinski, R. J., Andresson, T., Ferré-D'Amaré, A. R., Incarnato, D., and Schneekloth, J. S. (2023) Investigating the NRAS 5' UTR as a target for small molecules. Cell Chem Biol. 30, 643-657.e8
Bale, S., Baba, K., McCloskey, D. E., Pegg, A. E., and Ealick, S. E. (2010) Complexes of Thermotoga maritimaS-adenosylmethionine decarboxylase provide insights into substrate specificity. Acta Crystallogr D Biol Crystallogr. 66, 181-9
Bale, J. B., Gonen, S., Liu, Y., Sheffler, W., Ellis, D., Thomas, C., Cascio, D., Yeates, T. O., Gonen, T., King, N. P., and Baker, D. (2016) Accurate design of megadalton-scale two-component icosahedral protein complexes. Science. 353, 389-94

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