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Bale, J. B., Park, R. U., Liu, Y., Gonen, S., Gonen, T., Cascio, D., King, N. P., Yeates, T. O., and Baker, D. (2015) Structure of a designed tetrahedral protein assembly variant engineered to have improved soluble expression. Protein Sci. 24, 1695-701
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
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
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
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
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
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
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
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
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
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, 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
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
Baconguis, I., and Gouaux, E. (2012) Structural plasticity and dynamic selectivity of acid-sensing ion channel-spider toxin complexes. Nature. 489, 400-5
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
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
Baca, C. F., Yu, Y., Rostøl, J. T., Majumder, P., Patel, D. J., and Marraffini, L. A. (2024) The CRISPR effector Cam1 mediates membrane depolarization for phage defence. Nature. 10.1038/s41586-023-06902-y
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
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
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Aziz, F., Reddy, K., Vega, V. Fernandez, Dey, R., Hicks, K. A., Rao, S., Jordan, L. Ortiz, Smith, E., Shumate, J., Scampavia, L., Carpino, N., Spicer, T. P., and French, J. B. (2024) Rebamipide and Derivatives are Potent, Selective Inhibitors of Histidine Phosphatase Activity of the Suppressor of T Cell Receptor Signaling Proteins. J Med Chem. 67, 1949-1960
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
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

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