|
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 NCRR (National Center for Research Resources). 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. |
Recent Highlights10/26/2012Marcia, M., and Pyle, A.M. (2012) 09/19/2012Baconguis, I., and Gouaux, E. (2012) Structural plasticity and dynamic selectivity of acid-sensing ion channel-spider toxin complexes, Nature 489, 400-405. 06/21/2012Nakanishi, K., Weinberg, D. E., Bartel, D. P., and Patel, D. J. (2012) Structure of yeast Argonaute with guide RNA, Nature 486, 368-374. 05/25/2012Sosa, B. A., Rothballer, A., Kutay, U., and Schwartz, T. U. (2012) LINC Complexes Form by Binding of Three KASH Peptides to Domain Interfaces of Trimeric SUN Proteins, Cell 149, 1035-1047. 05/25/2012Hattori, M., and Gouaux, E. (2012) Molecular mechanism of ATP binding and ion channel activation in P2X receptors, Nature 485, 207-212. 05/18//2012Polikanov, Y. S., Blaha, G. M., and Steitz, T. A. (2012) How hibernation factors RMF, HPF, and YfiA turn off protein synthesis, Science 336, 915-918. 04/18/2012Kung, Y., Ando, N., Doukov, T. I., Blasiak, L. C., Bender, G., Seravalli, J., Ragsdale, S. W., and Drennan, C. L. (2012) Visualizing molecular juggling within a B12-dependent methyltransferase complex, Nature 484, 265-269. 03/19/2012Laganowsky, A., Liu, C., Sawaya, M. R., Whitelegge, J. P., Park, J., Zhao, M., Pensalfini, A., Soriaga, A. B., Landau, M., Teng, P. K., Cascio, D., Glabe, C., and Eisenberg, D. (2012) Atomic view of a toxic amyloid small oligomer, Science 335, 1228-1231. 01/27/2012Brohawn, S. G., del Marmol, J., and MacKinnon, R. (2012) Crystal structure of the human K2P TRAAK, a lipid- and mechano-sensitive K+ ion channel, Science 335, 436-441. Comment: Poulsen, H., and Nissen, P. (2012) Structural biology. The inner workings of a dynamic duo, Science 335, 416-417. 11/11/2011Scott, D. C., Monda, J. K., Bennett, E. J., Harper, J. W., and Schulman, B. A. (2011) N-Terminal Acetylation Acts as an Avidity Enhancer Within an Interconnected Multiprotein Complex, Science 334, 674-678. 08/12/2011Hu, J., Xue, Y., Lee, S., and Ha, Y. (2011) The crystal structure of GXGD membrane protease FlaK, Nature 475, 528-531 Highlights in C&E News. |
|
© 2005 Northeastern Collaborative Access Team Webmaster: Cyndi Salbego |
||