NECAT Beamline

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.

    NIGMS at a Glance.

    Supported by:

    National Institutes of Health
    National Institute of General Medical Sciences

    Publications from the Pilatus 6MF Detector

    (funded by grant S10RR029205 from the National Center of Research Resources of the National Institutes of Health)


    Battaglia, R. A., Price, I. R., and Ke, A. (2017) Structural Basis for Guanidine Sensing by the ykkC Family of Riboswitches, RNA.

    Chen, H., Coseno, M., Ficarro, S. B., Mansueto, M. S., Komazin-Meredith, G., Boissel, S., Filman, D. J., Marto, J. A., Hogle, J. M., and Coen, D. M. (2017) A Small Covalent Allosteric Inhibitor of Human Cytomegalovirus DNA Polymerase Subunit Interactions, ACS Infect Dis 3, 112-118.

    Crochet, R. B., Kim, J. D., Lee, H., Yim, Y. S., Kim, S. G., Neau, D., and Lee, Y. H. (2017) Crystal Structure of Heart 6-Phosphofructo-2-Kinase/Fructose-2,6-Bisphosphatase (PFKFB2) and the Inhibitory Influence of Citrate on Substrate Binding, Proteins 85, 117-124.

    Dang, B., Shen, R., Kubota, T., Mandal, K., Bezanilla, F., Roux, B., and Kent, S. B. (2017) Inversion of the Side-Chain Stereochemistry of Indvidual Thr or Ile Residues in a Protein Molecule: Impact on the Folding, Stability, and Structure of the ShK Toxin, Angew Chem Int Ed Engl 56, 3324-3328.

    Dhayalan, B., Mandal, K., Rege, N., Weiss, M. A., Eitel, S. H., Meier, T., Schoenleber, R. O., and Kent, S. B. (2017) Scope and Limitations of Fmoc Chemistry SPPS-Based Approaches to the Total Synthesis of Insulin Lispro via Ester Insulin, Chemistry 23, 1709-1716.

    Durzynska, I., Xu, X., Adelmant, G., Ficarro, S. B., Marto, J. A., Sliz, P., Uljon, S., and Blacklow, S. C. (2017) STK40 Is a Pseudokinase that Binds the E3 Ubiquitin Ligase COP1, Structure 25, 287-294.

    Gulati, S., Jastrzebska, B., Banerjee, S., Placeres, A. L., Miszta, P., Gao, S., Gunderson, K., Tochtrop, G. P., Filipek, S., Katayama, K., Kiser, P. D., Mogi, M., Stewart, P. L., and Palczewski, K. (2017) Photocyclic behavior of rhodopsin induced by an atypical isomerization mechanism, Proc Natl Acad Sci U S A.

    Hoffer, E. D., Miles, S. J., and Dunham, C. M. (2017) The structure and function of Mycobacterium tuberculosis MazF-mt6 provides insights into conserved features of MazF endonucleases, J Biol Chem.

    Luo, S., and Tong, L. (2017) Molecular mechanism for the regulation of yeast separase by securin, Nature 542, 255-259.

    Lv, Z., Rickman, K. A., Yuan, L., Williams, K., Selvam, S. P., Woosley, A. N., Howe, P. H., Ogretmen, B., Smogorzewska, A., and Olsen, S. K. (2017) S. pombe Uba1-Ubc15 Structure Reveals a Novel Regulatory Mechanism of Ubiquitin E2 Activity, Mol Cell 65, 699-714 e696.

    Nguyen, L. A., Wang, J., and Steitz, T. A. (2017) Crystal structure of Pistol, a class of self-cleaving ribozyme, Proc Natl Acad Sci U S A.

    Powers, R. E., Gaudet, R., and Sotomayor, M. (2017) A Partial Calcium-Free Linker Confers Flexibility to Inner-Ear Protocadherin-15, Structure.

    Ren, Y., Schmiege, P., and Blobel, G. (2017) Structural and biochemical analyses of the DEAD-box ATPase Sub2 in association with THO or Yra1, Elife 6.

    Schormann, N., Ayres, C. A., Fry, A., Green, T. J., Banerjee, S., Ulett, G. C., and Chattopadhyay, D. (2016) Crystal Structures of Group B Streptococcus Glyceraldehyde-3-Phosphate Dehydrogenase: Apo-Form, Binary and Ternary Complexes, PLoS One 11, e0165917.

    Su, M., Li, Y., Wyborny, S., Neau, D., Chakravarthy, S., Levine, B., Colbert, C. L., and Sinha, S. C. (2017) BECN2 interacts with ATG14 through a metastable coiled-coil to mediate autophagy, Protein Sci.

    Tararina, M. A., Janda, K. D., and Allen, K. N. (2016) Structural Analysis Provides Mechanistic Insight into Nicotine Oxidoreductase from Pseudomonas putida, Biochemistry 55, 6595-6598.

    Tayeb-Fligelman, E., Tabachnikov, O., Moshe, A., Goldshmidt-Tran, O., Sawaya, M. R., Coquelle, N., Colletier, J. P., and Landau, M. (2017) The cytotoxic Staphylococcus aureus PSMα3 reveals a cross-alpha amyloid-like fibril, Science 355, 831-833.

    Waldhart, G. W., Mankad, N. P., and Santarsiero, B. D. (2016) Improvements to the Practical Usability of the "Crystalline Sponge" Method for Organic Structure Determination, Org Lett 18, 6112-6115.




    AhYoung, A. P., Koehl, A., Vizcarra, C. L., Cascio, D., and Egea, P. F. (2016) Structure of a Putative Clps N-End Rule Adaptor Protein from the Malaria Pathogen Plasmodium Falciparum, Protein Sci. 25, 689-701.

    Ardiccioni, C., Clarke, O. B., Tomasek, D., Issa, H. A., von Alpen, D. C., Pond, H. L., Banerjee, S., Rajashankar, K. R., Liu, Q., Guan, Z., Li, C., Kloss, B., Bruni, R., Kloppmann, E., Rost, B., Manzini, M. C., Shapiro, L., and Mancia, F. (2016) Structure of the Polyisoprenyl-Phosphate Glycosyltransferase Gtrb and Insights into the Mechanism of Catalysis, Nat. Commun. 7, 10175.

    Atkison, J. H., Parnham, S., Marcotte, W. R., Jr., and Olsen, S. K. (2016) Crystal Structure of the Nephila clavipes Major Ampullate Spidroin 1A N-terminal Domain Reveals Plasticity at the Dimer Interface, J Biol Chem 291, 19006-19017.

    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, 389-394.

    Baranovskiy, A. G., Babayeva, N. D., Zhang, Y., Gu, J., Suwa, Y., Pavlov, Y. I., and Tahirov, T. H. (2016) Mechanism of Concerted Rna-DNA Primer Synthesis by the Human Primosome, J. Biol. Chem. 291, 10006-10020.

    Bodea, S., Funk, M. A., Balskus, E. P., and Drennan, C. L. (2016) Molecular Basis of C-N Bond Cleavage by the Glycyl Radical Enzyme Choline Trimethylamine-Lyase, Cell Chem Biol [Epub ahead of print].

    Blower, T. R., Williamson, B. H., Kerns, R. J., and Berger, J. M. (2016) Crystal Structure and Stability of Gyrase-Fluoroquinolone Cleaved Complexes from Mycobacterium Tuberculosis, Proc. Natl. Acad. Sci. U. S. A. 113, 1706-1713.

    Buffalo, C. Z., Bahn-Suh, A. J., Hirakis, S. P., Biswas, T., Amaro, R. E., Nizet, V., and Ghosh, P. (2016) Conserved patterns hidden within group A Streptococcus M protein hypervariability recognize human C4b-binding protein, Nat Microbiol 1, 16155.

    Chatterjee, D., Sanchez, A. M., Goldgur, Y., Shuman, S., and Schwer, B. (2016) Transcription of Lncrna Prt, Clustered Prt Rna Sites for Mmi1 Binding, and Rna Polymerase Ii Ctd Phospho-Sites Govern the Repression of Pho1 Gene Expression under Phosphate-Replete Conditions in Fission Yeast, RNA 22, 1011-1025.

    Chen, M., Chou, W. K., Al-Lami, N., Faraldos, J. A., Allemann, R. K., Cane, D. E., and Christianson, D. W. (2016) Probing the Role of Active Site Water in the Sesquiterpene Cyclization Reaction Catalyzed by Aristolochene Synthase, Biochemistry 55, 2864-2874.

    Cho, J., Lee, C.-J., Zhao, J., Young, H. E., and Zhou, P. (2016) Structure of the essential Haemophilus influenzae UDP-diacylglucosamine pyrophosphohydrolase LpxH in lipid A biosynthesis, Nature Microbiology 1, 16154.

    Chowdhury, C., Chun, S., Sawaya, M. R., Yeates, T. O., and Bobik, T. A. (2016) The Function of the Pduj Microcompartment Shell Protein Is Determined by the Genomic Position of Its Encoding Gene, Mol Microbiol 101, 770-783.

    Chung, B. C., Mashalidis, E. H., Tanino, T., Kim, M., Matsuda, A., Hong, J., Ichikawa, S., and Lee, S. Y. (2016) Structural Insights into Inhibition of Lipid I Production in Bacterial Cell Wall Synthesis, Nature 533, 557-5690.

    Coleman, J. A., Green, E. M., and Gouaux, E. (2016) X-Ray Structures and Mechanism of the Human Serotonin Transporter, Nature 532, 334-339.

    Coloma, J., Jain, R., Rajashankar, Kanagalaghatta R., Garcia-Sastre, A., and Aggarwal, Aneel K. (2016) Structures of NS5 Methyltransferase from Zika Virus, Cell Reports.

    Cooper, S. R., Jontes, J. D., and Sotomayor, M. (2016) Structural determinants of adhesion by Protocadherin-19 and implications for its role in epilepsy, Elife 5.

    Dharmaiah, S., Bindu, L., Tran, T. H., Gillette, W. K., Frank, P. H., Ghirlando, R., Nissley, D. V., Esposito, D., McCormick, F., Stephen, A. G., and Simanshu, D. K. (2016) Structural basis of recognition of farnesylated and methylated KRAS4b by PDEdelta, Proc Natl Acad Sci U S A 113, E6766-E6775.

    Dhakshnamoorthy, B., Rohaim, A., Rui, H., Blachowicz, L., and Roux, B. (2016) Structural and functional characterization of a calcium-activated cation channel from Tsukamurella paurometabola, Nat Commun 7, 12753.

    Dhayalan, B., Fitzpatrick, A., Mandal, K., Whittaker, J., Weiss, M., Tokmakoff, A., and Kent, S. (2016) Efficient Total Chemical Synthesis of 13c=18o Isotopomers of Human Insulin for Isotope-Edited Ftir, Chembiochem 17, 415-420.

    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. (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, E4151-4160.

    Dowling, D. P., Miles, Z. D., Kohrer, C., Maiocco, S. J., Elliott, S. J., Bandarian, V., and Drennan, C. L. (2016) Molecular basis of cobalamin-dependent RNA modification, Nucleic Acids Res.


    Feliciano, P. R., Drennan, C. L., and Nonato, M. C. (2016) Crystal structure of an Fe-S cluster-containing fumarate hydratase enzyme from Leishmania major reveals a unique protein fold, Proc Natl Acad Sci U S A.

    Gagnon, M. G., Lin, J., and Steitz, T. A. (2016) Elongation Factor 4 Remodels the a-Site Trna on the Ribosome, Proc. Natl. Acad. Sci. U. S. A. 113, 4994–4999.

    Gagnon, M. G., Roy, R. N., Lomakin, I. B., Florin, T., Mankin, A. S., and Steitz, T. A. (2016) Structures of Proline-Rich Peptides Bound to the Ribosome Reveal a Common Mechanism of Protein Synthesis Inhibition, Nucleic Acids Res. 44, 2439-2450.

    Gantt, S. M. F., Decroos, C., Lee, M. S., Gullett, L. E., Bowman, C. M., Christianson, D. W., and Fierke, C. A. (2016) General Base-General Acid Catalysis in Human Histone Deacetylase 8, Biochemistry 55, 820–832.

    Gao, P., Yang, H., Rajashankar, K. R., Huang, Z., and Patel, D. J. (2016) Type V CRISPR-Cas Cpf1 endonuclease employs a unique mechanism for crRNA-mediated target DNA recognition,Cell Res 26, 901-913.

    Geronimo, I., Denning, C. A., Rogers, W. E., Othman, T., Huxford, T., Heidary, D. K., Glazer, E. C., and Payne, C. M. (2016) Effect of Mutation and Substrate Binding on the Stability of Cytochrome P450bm3 Variants, Biochemistry 55, 3594-3606.

    Gibson, M. I., Chen, P. Y., Johnson, A. C., Pierce, E., Can, M., Ragsdale, S. W., and Drennan, C. L. (2016) One-Carbon Chemistry of Oxalate Oxidoreductase Captured by X-Ray Crystallography, Proc. Natl. Acad. Sci. U.S.A. 113, 320-325.

    Goodman, Kerry M., Rubinstein, R., Thu, Chan A., Bahna, F., Mannepalli, S., Ahlsén, G., Rittenhouse, C., Maniatis, T., Honig, B., and Shapiro, L. (2016) Structural Basis of Diverse Homophilic Recognition by Clustered α- and β-Protocadherins, Neuron 90, 709-723.

    Goodman, K. M., Rubinstein, R., Thu, C. A., Mannepalli, S., Bahna, F., Ahlsen, G., Rittenhouse, C., Maniatis, T., Honig, B., and Shapiro, L. (2016) γ-Protocadherin structural diversity and functional implications, Elife 5.

    Gorelik, M., Orlicky, S., Sartori, M. A., Tang, X., Marcon, E., Kurinov, I., Greenblatt, J. F., Tyers, M., Moffat, J., Sicheri, F., and Sidhu, S. S. (2016) Inhibition of Scf Ubiquitin Ligases by Engineered Ubiquitin Variants That Target the Cul1 Binding Site on the Skp1-F-Box Interface, Proc. Natl. Acad. Sci. U.S.A. 113, 3527–3532.

    Hayes, R. P., Xiao, Y., Ding, F., van Erp, P. B. G., Rajashankar, K., Bailey, S., Wiedenheft, B., and Ke, A. (2016) Structural Basis for Promiscuous Pam Recognition in Type I–E Cascade from E. Coli, Nature 530, 499-503.

    Hicks, K. A., and Ealick, S. E. (2016) Biochemical and Structural Characterization of Klebsiella Pneumoniae Oxamate Amidohydrolase in the Uric Acid Degradation Pathway, Acta Crystallogr D Struct Biol 72, 808-816.

    Hicks, K. A., Yuen, M. E., Zhen, W. F., Gerwig, T. J., Story, R. W., Kopp, M. C., and Snider, M. J. (2016) Structural and Biochemical Characterization of 6-Hydroxynicotinic Acid 3-Monooxygenase, a Novel Decarboxylative Hydroxylase Involved in Aerobic Nicotinate Degradation, Biochemistry 55, 3432-3446.

    Huang, H., Deng, Z., Vladimirova, O., Wiedmer, A., Lu, F., Lieberman, P. M., and Patel, D. J. (2016) Structural basis underlying viral hijacking of a histone chaperone complex, Nat Commun 7, 12707.

    Jorda, J., Leibly, D. J., Thompson, M. C., and Yeates, T. O. (2016) Structure of a Novel 13 Nm Dodecahedral Nanocage Assembled from a Redesigned Bacterial Microcompartment Shell Protein, Chem. Commun. (Camb) 52, 5041-5044.

    Kim, M., Sandford, E., Gatica, D., Qiu, Y., Liu, X., Zheng, Y., Schulman, B. A., Xu, J., Semple, I., Ro, S. H., Kim, B., Mavioglu, R. N., Tolun, A., Jipa, A., Takats, S., Karpati, M., Li, J. Z., Yapici, Z., Juhasz, G., Lee, J. H., Klionsky, D. J., and Burmeister, M. (2016) Mutation in Atg5 Reduces Autophagy and Leads to Ataxia with Developmental Delay, Elife 5, e12245.

    Kumar, N., Radhakrishnan, A., Su, C. C., Osteryoung, K. W., and Yu, E. W. (2016) Crystal Structure of a Conserved Domain in the Intermembrane Space Region of the Plastid Division Protein Arc6, Protein Sci. 25, 523-529.

    Lee, S. J., Ren, F., Zangerl-Plessl, E. M., Heyman, S., Stary-Weinzinger, A., Yuan, P., and Nichols, C. G. (2016) Structural basis of control of inward rectifier Kir2 channel gating by bulk anionic phospholipids, J Gen Physiol 148, 227-237.

    Leroy, E., Dusa, A., Colau, Motamedi, A., Cahu, X., Mouton, C., Huang, L. J., Shiau, A. K., and Constantinescu, S. N. (2016) Uncoupling Jak2 V617f Activation from Cytokine-Induced Signalling by Modulation of Jh2 Alphac Helix, Biochem. J. 473, 1579-1591.

    Liu, B., Zuo, Y., and Steitz, T. A. (2016) Structures of E. Coli Σs-Transcription Initiation Complexes Provide New Insights into Polymerase Mechanism, Proc. Natl. Acad. Sci. U. S. A. 113, 4051-4056.

    Lyubimov, A. Y., Uervirojnangkoorn, M., Zeldin, O. B., Zhou, Q., Zhao, M., Brewster, A. S., Michels-Clark, T., Holton, J. M., Sauter, N. K., Weis, W. I., and Brunger, A. T. (2016) Advances in X-ray free electron laser (XFEL) diffraction data processing applied to the crystal structure of the synaptotagmin-1 / SNARE complex, Elife 5.

    Mandal, K., Dhayalan, B., Avital-Shmilovici, M., Tokmakoff, A., and Kent, S. B. H. (2016) Crystallization of Enantiomerically Pure Proteins from Quasi-Racemic Mixtures: Structure Determination by X-Ray Diffraction of Isotope-Labeled Ester Insulin and Human Insulin, ChemBioChem 17, 421-425.

    Matsuyama, B. Y., Krasteva, P. V., Baraquet, C., Harwood, C. S., Sondermann, H., and Navarro, M. V. (2016) Mechanistic Insights into C-Di-Gmp-Dependent Control of the Biofilm Regulator Fleq from Pseudomonas Aeruginosa, Proc. Natl. Acad. U. S. A. 113, E209-218.

    Matthews, M. M., Thomas, J. M., Zheng, Y., Tran, K., Phelps, K. J., Scott, A. I., Havel, J., Fisher, A. J., and Beal, P. A. (2016) Structures of Human Adar2 Bound to Dsrna Reveal Base-Flipping Mechanism and Basis for Site Selectivity, Nat. Struct. Mol. Biol. 23, 426-433.

    McCoy, Jason G., Ren, Z., Stanevich, V., Lee, J., Mitra, S., Levin, Elena J., Poget, S., Quick, M., Im, W., and Zhou, M. (2016) The Structure of a Sugar Transporter of the Glucose Eiic Superfamily Provides Insight into the Elevator Mechanism of Membrane Transport, Structure 24, 956-964.

    McLaughlin, M. I., Lanz, N. D., Goldman, P. J., Lee, K. H., Booker, S. J., and Drennan, C. L. (2016) Crystallographic snapshots of sulfur insertion by lipoyl synthase, Proc Natl Acad Sci U S A.

    Mansoor, S. E., Lu, W., Oosterheert, W., Shekhar, M., Tajkhorshid, E., and Gouaux, E. (2016) X-ray structures define human P2X3 receptor gating cycle and antagonist action, Nature.

    Meisburger, S. P., Taylor, A. B., Khan, C. A., Zhang, S., Fitzpatrick, P. F., and Ando, N. (2016) Domain Movements Upon Activation of Phenylalanine Hydroxylase Characterized by Crystallography and Chromatography-Coupled Small-Angle X-Ray Scattering, J. Am. Chem. Soc. 138, 6506-6516.

    Melillo, B., Liang, S., Park, J., Schon, A., Courter, J. R., LaLonde, J. M., Wendler, D. J., Princiotto, A. M., Seaman, M. S., Freire, E., Sodroski, J., Madani, N., Hendrickson, W. A., and Smith, A. B., 3rd. (2016) Small-Molecule Cd4-Mimics: Structure-Based Optimization of Hiv-1 Entry Inhibition, ACS Med. Chem. Lett. 7, 330-334.

    Metrick, C. M., and Heldwein, E. E. (2016) Novel Structure and Unexpected Rna-Binding Ability of the C-Terminal Domain of Herpes Simplex Virus 1 Tegument Protein Ul21, J Virol 90, 5759-5769.

    Metrick, C. M., and Heldwein, E. E. (2016) The Novel Structure and Unexpected Rna-Binding Ability of the C-Terminal Domain of Hsv-1 Tegument Protein Ul21, J. Virol. 90, 5759-5769.

    Morales-Perez, C. L., Noviello, C. M., and Hibbs, R. E. (2016) X-ray structure of the human α4β2 nicotinic receptor, Nature 538, 411-415.

    Morgan, J. L., McNamara, J. T., Fischer, M., Rich, J., Chen, H. M., Withers, S. G., and Zimmer, J. (2016) Observing Cellulose Biosynthesis and Membrane Translocation in Crystallo, Nature 531, 329-334.

    Murn, J., Teplova, M., Zarnack, K., Shi, Y., and Patel, D. J. (2016) Recognition of Distinct Rna Motifs by the Clustered Ccch Zinc Fingers of Neuronal Protein Unkempt, Nat. Struct. Mol. Biol. 23, 16-23.

    Neumann, W., Xu, S., Sarosi, M. B., Scholz, M. S., Crews, B. C., Ghebreselasie, K., Banerjee, S., Marnett, L. J., and Hey-Hawkins, H. C. (2016) Nido-Dicarbaborate Induces Potent and Selective Inhibition of Cyclooxygenase-2, ChemMedChem 11, 175-178.

    Nicoludis, J. M., Vogt, B. E., Green, A. G., Scharfe, C. P., Marks, D. S., and Gaudet, R. (2016) Antiparallel protocadherin homodimers use distinct affinity- and specificity-mediating regions in cadherin repeats 1-4, Elife 5.

    Oyala, P. H., Ravichandran, K. R., Funk, M. A., Stucky, P. A., Stich, T. A., Drennan, C. L., Britt, R. D., and Stubbe, J. (2016) Biophysical Characterization of Fluorotyrosine Probes Site-Specifically Incorporated into Enzymes: E. coli Ribonucleotide Reductase As an Example, J Am. Chem. Soc. 138, 7951-7964.

    Pascolutti, R., Sun, X., Kao, J., Maute, R. L., Ring, A. M., Bowman, G. R., and Kruse, A. C. (2016) Structure and Dynamics of PD-L1 and an Ultra-High-Affinity PD-1 Receptor Mutant, Structure.

    Petrou, V. I., Herrera, C. M., Schultz, K. M., Clarke, O. B., Vendome, J., Tomasek, D., Banerjee, S., Rajashankar, K. R., Belcher Dufrisne, M., Kloss, B., Kloppmann, E., Rost, B., Klug, C. S., Trent, M. S., Shapiro, L., and Mancia, F. (2016) Structures of Aminoarabinose Transferase Arnt Suggest a Molecular Basis for Lipid a Glycosylation, Science 351, 608-612.

    Pierson, W. E., Hoffer, E. D., Keedy, H. E., Simms, C. L., Dunham, C. M., and Zaher, H. S. (2016) Uniformity of Peptide Release Is Maintained by Methylation of Release Factors, Cell Rep 17, 11-18.

    Rechkoblit, O., Gupta, Y. K., Malik, R., Rajashankar, K. R., Johnson, R. E., Prakash, L., Prakash, S., and Aggarwal, A. K. (2016) Structure and mechanism of human PrimPol, a DNA polymerase with primase activity, Sci Adv 2, e1601317.

    Ren, A., Vusurovic, N., Gebetsberger, J., Gao, P., Juen, M., Kreutz, C., Micura, R., and Patel, D. J. (2016) Pistol Ribozyme Adopts a Pseudoknot Fold Facilitating Site-Specific in-Line Cleavage, Nat Chem Biol 12, 702-708.

    Saotome, K., Singh, A. K., Yelshanskaya, M. V., and Sobolevsky, A. I. (2016) Crystal structure of the epithelial calcium channel TRPV6, Nature 534, 506-511.

    Saxton, R. A., Knockenhauer, K. E., Schwartz, T. U., and Sabatini, D. M. (2016) The apo-structure of the leucine sensor Sestrin2 is still elusive, Sci Signal 9, ra92.

    Saxton, R. A., Knockenhauer, K. E., Wolfson, R. L., Chantranupong, L., Pacold, M. E., Wang, T., Schwartz, T. U., and Sabatini, D. M. (2016) Structural Basis for Leucine Sensing by the Sestrin2-Mtorc1 Pathway, Science 351, 53-58.

    Schmidt, F. I., Lu, A., Chen, J. W., Ruan, J., Tang, C., Wu, H., and Ploegh, H. L. (2016) A Single Domain Antibody Fragment That Recognizes the Adaptor Asc Defines the Role of Asc Domains in Inflammasome Assembly, J. Exp. Med. 213, 771–790.

    Schmidt, H. R., Zheng, S., Gurpinar, E., Koehl, A., Manglik, A., and Kruse, A. C. (2016) Crystal Structure of the Human Σ1 Receptor, Nature 532, 527-530.

    Schureck, M. A., Repack, A., Miles, S. J., Marquez, J., and Dunham, C. M. (2016) Mechanism of endonuclease cleavage by the HigB toxin, Nucleic Acids Res [Epub ahead of print].

    Shao, Y., Huang, H., Qin, D., Li, N. S., Koide, A., Staley, J. P., Koide, S., Kossiakoff, A. A., and Piccirilli, J. A. (2016) Specific Recognition of a Single-stranded RNA Sequence by a Synthetic Antibody Fragment, J Mol Biol.

    Shan, C. M., Wang, J., Xu, K., Chen, H., Yue, J. X., Andrews, S., Moresco, J. J., Yates, J. R., Nagy, P. L., Tong, L., and Jia, S. (2016) A histone H3K9M mutation traps histone methyltransferase Clr4 to prevent heterochromatin spreading, Elife 5.

    Silvaroli, J. A., Arne, J. M., Chelstowska, S., Kiser, P. D., Banerjee, S., and Golczak, M. (2016) Ligand Binding Induces Conformational Changes in Human Cellular Retinol-Binding Protein 1 (Crbp1) Revealed by Atomic Resolution Crystal Structures, J. Biol. Chem. 291, 8528-8540.

    Tabackman, A. A., Frankson, R., Marsan, E. S., Perry, K., and Cole, K. E. (2016) Structure of 'Linkerless' Hydroxamic Acid Inhibitor-HDAC8 Complex Confirms the Formation of an Isoform-Specific Subpocket, J Struct. Biol. 195, 373-378.

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