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.
National Institutes of Health
Synchrotron radiation is essential for maintaining a competitive program in X-ray crystallography. The APS is one of three high-energy, third generation synchrotron sources, the other two being the ESRF and SPRING-8 . The APS undulator sources provide the highest brilliance available in the United States. In addition, the APS provides a support structure, including laboratory and office modules, that facilitates biological studies.
In order to gain access to such an important research resource, researchers from Columbia, Cornell, Harvard, Memorial Sloan-Kettering Cancer Center, Massachusetts Institute of Technology, Rockefeller, and Yale formed a collaboration, NE-CAT, to construct and operate a facility at APS. Having obtained the needed funding commitments from the NIH National Center for Research Resources and the participating institutions, the formal Memorandum of Understanding between APS and NE-CAT was signed on May 3, 2002.
The NE-CAT scientists are involved in a wide range of research projects. Particular emphases are placed on signal transduction, DNA transcription initiation and regulation, cell cycle regulation, virus structure and function, membrane proteins, protein folding, and enzyme structure and function. Many of the research projects focus on how biological molecules interact to form large macromolecular complexes. The macromolecules studied by NE-CAT members often involve large unit cells, small crystals, weakly diffracting crystals, and crystals with weak anomalous scattering, requiring ultra high resolution data.
The main technological R&D thrust will be to develop a sector in which the beamline components, instrumentation and software are optimized for the crystallography of technically challenging molecular structures. Specific areas of technological R&D or innovation will include:
NE-CAT will operate a user program consistent with the guidelines of the APS and NIGMS (National Institute of General Medical Sciences). The user program will be fully supported, with each experimental station staffed 24 hours a day. The support, which will be provided by a combination of BS/MS technical staff, postdocs and staff scientists, will assist in all aspects of data collection and analysis. Laboratory and office space will be provided for crystal growth, sample preparation, data processing, etc.
The NE-CAT consortium plans the following educational features:
1. On-site training for individual users.
August 23, 2017
Zhou, Q., Zhou, P., Wang, A. L., Wu, D., Zhao, M., Sudhof, T. C., and Brunger, A. T. (2017) The primed SNARE-complexin-synaptotagmin complex for neuronal exocytosis, Nature [Epub ahead of print].
June 9, 2017
Yang, H., and Patel, D. J. (2017) Inhibition Mechanism of an Anti-CRISPR Suppressor AcrIIA4 Targeting SpyCas9, Mol Cell 67, 117-127 e115.
July 20, 2017
Wohlever, M. L., Mateja, A., McGilvray, P. T., Day, K. J., and Keenan, R. J. (2017) Msp1 Is a Membrane Protein Dislocase for Tail-Anchored Proteins, Mol Cell 67, 194-202 e196.
May 26, 2017
Feklistov, A., Bae, B., Hauver, J., Lass-Napiorkowska, A., Kalesse, M., Glaus, F., Altmann, K. H., Heyduk, T., Landick, R., and Darst, S. A. (2017) RNA polymerase motions during promoter melting, Science 356, 863-866.
April 14, 2017
Stanek, K. A., Patterson-West, J., Randolph, P. S., and Mura, C. (2017) Crystal structure and RNA-binding properties of an Hfq homolog from the deep-branching Aquificae: conservation of the lateral RNA-binding mode, Acta Crystallogr D Struct Biol 73, 294-315.
March 29, 2017
Yao, G., Lam, K. H., Perry, K., Weisemann, J., Rummel, A., and Jin, R. (2017) Crystal Structure of the Receptor-Binding Domain of Botulinum Neurotoxin Type HA, Also Known as Type FA or H, Toxins (Basel) 9.
February 17, 2017
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.
February 13, 2017
Shi, K., Carpenter, M. A., Banerjee, S., Shaban, N. M., Kurahashi, K., Salamango, D. J., McCann, J. L., Starrett, G. J., Duffy, J. V., Demir, O., Amaro, R. E., Harki, D. A., Harris, R. S., and Aihara, H. (2017) Structural basis for targeted DNA cytosine deamination and mutagenesis by APOBEC3A and APOBEC3B, Nat Struct Mol Biol 24, 131-139.
January 31, 2017
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.
January 11, 2017
Kuk, A. C., Mashalidis, E. H., and Lee, S. Y. (2016) Crystal structure of the MOP flippase MurJ in an inward-facing conformation, Nat Struct Mol Biol, [epub ahead of print]
December 15, 2017
Yang, H., Gao, P., Rajashankar, K. R., and Patel, D. J. (2016) PAM-Dependent Target DNA Recognition and Cleavage by C2c1 CRISPR-Cas Endonuclease, Cell 167, 1814-1828 e1812.
December 6, 2016
Bozzi, A. T., Bane, L. B., Weihofen, W. A., Singharoy, A., Guillen, E. R., Ploegh, H. L., Schulten, K., and Gaudet, R. (2016) Crystal Structure and Conformational Change Mechanism of a Bacterial Nramp-Family Divalent Metal Transporter, Structure 24, 2102-2114.
November 20, 2016
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 44, 9965-9976.
November 3, 2016
Dimitrova, Yoana N., Jenni, S., Valverde, R., Khin, Y., and Harrison, Stephen C. (2016) Structure of the MIND Complex Defines a Regulatory Focus for Yeast Kinetochore Assembly, Cell 167, 1014-1027 e1012.
October 21, 2016
Rechkoblit, O., Gupta, Y.K., Malik, R., Rajashankar, K.R., Johnson, R.E., Prakash, L., Prakash, S., Aggarwal, A.K. (2016) Structure and mechanism of human PrimPol, a DNA polymerase with primase activity, Science Advances, 2(10) e1601317
October 20, 2016
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