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.
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    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 Institue of General Medical Sciences

    Publications based in part upon data collected at the NE-CAT beamlines at the Advanced Photon Source
    (reverse chronological order)

    Unciuleac, M. C., Goldgur, Y., and Shuman, S. (2017) Two-metal versus one-metal mechanisms of lysine adenylylation by ATP-dependent and NAD+-dependent polynucleotide ligases, Proc Natl Acad Sci U S A.
    https://www.ncbi.nlm.nih.gov/pubmed/28223499

    Powers, R. E., Gaudet, R., and Sotomayor, M. (2017) A Partial Calcium-Free Linker Confers Flexibility to Inner-Ear Protocadherin-15, Structure.
    https://www.ncbi.nlm.nih.gov/pubmed/28238533

    Campbell, E. A., Kamath, S., Rajashankar, K. R., Wu, M., and Darst, S. A. (2017) Crystal structure of Aquifex aeolicus sigmaN bound to promoter DNA and the structure of sigmaN-holoenzyme, Proc Natl Acad Sci U S A.
    https://www.ncbi.nlm.nih.gov/pubmed/28223493

    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.
    https://www.ncbi.nlm.nih.gov/pubmed/28218432

    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.
    https://www.ncbi.nlm.nih.gov/pubmed/28232575

    Kim, S. K., Barron, L., Hinck, C. S., Petrunak, E. M., Cano, K. E., Thangirala, A., Iskra, B., Brothers, M., Vonberg, M., Leal, B., Richter, B., Kodali, R., Taylor, A. B., Du, S., Barnes, C. O., Sulea, T., Calero, G., Hart, P. J., Hart, M. J., Demeler, B., and Hinck, A. P. (2017) An Engineered TGF-beta Monomer that Functions as a Dominant Negative to Block TGF-beta Signaling, J Biol Chem.
    https://www.ncbi.nlm.nih.gov/pubmed/28228478

    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.
    https://www.ncbi.nlm.nih.gov/pubmed/27934356

    Walhart, G. W., Santarsiero, B. D., Orjala, J., and Mankad, N. P. (2016) Improvements in the practical utility of the "crystalline sponge" method for structural characterization of natural products, Planta Med 81, S1-S381.
    https://www.ncbi.nlm.nih.gov/pubmed/27975465

    De Schutter, J. W., Morrison, J. P., Morrison, M. J., Ciulli, A., and Imperiali, B. (2017) Targeting Bacillosamine Biosynthesis in Bacterial Pathogens: Development of Inhibitors to a Bacterial Amino-Sugar Acetyltransferase from Campylobacter jejuni, J Med Chem.
    https://www.ncbi.nlm.nih.gov/pubmed/28182413

    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.
    https://www.ncbi.nlm.nih.gov/pubmed/28162934

    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 6.
    https://www.ncbi.nlm.nih.gov/pubmed/28067618

    Hubin, E. A. (2016), Structural and functional studies of mycobacterial general transcription factors RbpA and CarD, The Rockefeller University,

    Lees, J. A., Messa, M., Sun, E. W., Wheeler, H., Torta, F., Wenk, M. R., De Camilli, P., and Reinisch, K. M. (2017) Lipid transport by TMEM24 at ER-plasma membrane contacts regulates pulsatile insulin secretion, Science 355.
    https://www.ncbi.nlm.nih.gov/pubmed/28209843

    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.
    https://www.ncbi.nlm.nih.gov/pubmed/27933790

    Wang, L., Chakravarthy, S., and Verdine, G. L. (2017) Structural Basis for the Lesion-scanning Mechanism of the Bacterial MutY DNA Glycosylase, J Biol Chem.
    https://www.ncbi.nlm.nih.gov/pubmed/28130451

    Battaglia, R. A., Price, I. R., and Ke, A. (2017) Structural Basis for Guanidine Sensing by the ykkC Family of Riboswitches, RNA.
    https://www.ncbi.nlm.nih.gov/pubmed/28096518

    Zhu, Y., Luo, S., Sabo, Y., Wang, C., Tong, L., and Goff, S. P. (2017) Heme Oxygenase 2 Binds Myristate to Regulate Retrovirus Assembly and TLR4 Signaling, Cell Host Microbe 21, 220-230.
    https://www.ncbi.nlm.nih.gov/pubmed/28132836

    Luo, S., and Tong, L. (2017) Molecular mechanism for the regulation of yeast separase by securin, Nature 542, 255-259.
    https://www.ncbi.nlm.nih.gov/pubmed/28146474

    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.
    https://www.ncbi.nlm.nih.gov/pubmed/27875551

    Karasawa, A., and Kawate, T. (2016) Structural basis for subtype-specific inhibition of the P2X7 receptor, Elife 5.
    https://www.ncbi.nlm.nih.gov/pubmed/27935479

    Lee, W. G., Chan, A. H., Spasov, K. A., Anderson, K. S., and Jorgensen, W. L. (2016) Design, Conformation, and Crystallography of 2-Naphthyl Phenyl Ethers as Potent Anti-HIV Agents, ACS Med Chem Lett 7, 1156-1160.
    https://www.ncbi.nlm.nih.gov/pubmed/27994756

    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.
    https://www.ncbi.nlm.nih.gov/pubmed/27905149

    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.
    https://www.ncbi.nlm.nih.gov/pubmed/28089446

    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 114, 1021-1026.
    https://www.ncbi.nlm.nih.gov/pubmed/28096403

    Bruender, N. A., Grell, T. A., Dowling, D. P., McCarty, R. M., Drennan, C. L., and Bandarian, V. (2017) 7-Carboxy-7-deazaguanine synthase - A radical S-adenosyl-L-methionine enzyme with polar tendencies, J Am Chem Soc 139, 1912-1920.
    https://www.ncbi.nlm.nih.gov/pubmed/28045519

    Krotee, P., Rodriguez, J. A., Sawaya, M. R., Cascio, D., Reyes, F. E., Shi, D., Hattne, J., Nannenga, B. L., Oskarsson, M. E., Philipp, S., Griner, S., Jiang, L., Glabe, C. G., Westermark, G. T., Gonen, T., and Eisenberg, D. S. (2017) Atomic structures of fibrillar segments of hIAPP suggest tightly mated beta-sheets are important for cytotoxicity, Elife 6.
    https://www.ncbi.nlm.nih.gov/pubmed/28045370

    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.
    https://www.ncbi.nlm.nih.gov/pubmed/28059701

    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.

    https://www.ncbi.nlm.nih.gov/pubmed/27802586

     

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