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
The Northeastern Collaborative Access Team (NE-CAT) is funded by its member institutions and the National Institute of General Medical Sciences (NIGMS) to operate synchrotron X-ray beamlines to address technically challenging problems in structural biology. These beamlines are an important resource for NE-CAT's institutional members as well as the national research community. NE-CAT provides 50% of the available beam time to the national user community. These beamlines have been developed using the extremely high-brilliance X-ray sources provided by the novel dual-canted undulators of the Advanced Photon Source (APS) at the Argonne National Laboratory. The optical trains for NE-CAT’s two canted-undulator beamlines are schematically shown below.
Both undulator beamlines, 24-ID-C and 24-ID-E, are in full operation providing exceptionally stable well collimated X-ray beams and are optimized for microdiffraction crystallographic research. The 24-ID-C beamline is a variable-energy beamline providing X-rays from 6.5 to 20 keV. The 24-ID-E beamline is a fixed–energy microdiffraction beamline providing X-rays at 12.66 keV. Detailed descriptions of the beamlines can be found under “Facilities”.
The user end stations for all the beamlines are fully equipped with state-of-the-art instrumentation for its users. Both undulator beamlines are equipped with MD2 microdiffractometers. The MD2 provides exceptionally well collimated beams from 5 microns to 100 microns in diameter and has sample visualization systems capable of visualizing micron-sized crystals. For data collection, both beamlines are equipped with very large-area CCD-based ADSC Quantum 315 detectors connected to a data storage system currently with a capacity of 39TB. The data acquisition systems are designed for very fast data acquisition, capable of taking exposures as short as 250 msec, with a dead time of 2 sec for un-binned images and 1 sec for binned images. Advanced Light Source (ALS)-type robotic sample auto-mount systems are available on both beamlines to automatically mount and dismount crystals. This robotic system makes screening large numbers of crystals much faster and easier. Users of the beamlines are supported by experienced crystallographers and have access to a full suite of on-line and off-line data processing software to analyze their data and solve macromolecular structures. A fully equipped chemistry laboratory is also available for users. Shown below are photographs of the two undulator-based user endstations.
July 24, 2014
Wasmuth, E. V., Januszyk, K., and Lima, C. D. (2014) Structure of an Rrp6-RNA exosome complex bound to poly(A) RNA, Nature 511, 435-439.
July 3, 2014
Clayton, G. M., Wang, Y., Crawford, F., Novikov, A., Wimberly, B. T., Kieft, J. S., Falta, M. T., Bowerman, N. A., Marrack, P., Fontenot, A. P., Dai, S., and Kappler, J. W. (2014) Structural basis of chronic beryllium disease: linking allergic hypersensitivity and autoimmunity, Cell 158, 132-142.
June 26, 2014
Schauder, C. M., Wu, X., Saheki, Y., Narayanaswamy, P., Torta, F., Wenk, M. R., De Camilli, P., and Reinisch, K. M. (2014) Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer, Nature 510, 552-555.
June 20, 2014
Lee, K., Zhong, X., Gu, S., Kruel, A. M., Dorner, M. B., Perry, K., Rummel, A., Dong, M., and Jin, R. (2014) Molecular basis for disruption of E-cadherin adhesion by botulinum neurotoxin A complex, Science 344, 1405-1410.
June 19th, 2014
Sasaki, E., Zhang, X., Sun, H. G., Lu, M. Y., Liu, T. L., Ou, A., Li, J. Y., Chen, Y. H., Ealick, S. E., and Liu, H. W. (2014) Co-opting sulphur-carrier proteins from primary metabolic pathways for 2-thiosugar biosynthesis, Nature 510, 427-431.
Scott, Daniel C., Sviderskiy, Vladislav O., Monda, Julie K., Lydeard, John R., Cho, Shein E., Harper, J. W., and Schulman, Brenda A. (2014) Structure of a RING E3 Trapped in Action Reveals Ligation Mechanism for the Ubiquitin-like Protein NEDD8, Cell 157, 1671-1684
June 13, 2014
Xu, K., Wu, Z., Renier, N., Antipenko, A., Tzvetkova-Robev, D., Xu, Y., Minchenko, M., Nardi-Dei, V., Rajashankar, K. R., Himanen, J., Tessier-Lavigne, M., and Nikolov, D. B. (2014) Structures of netrin-1 bound to two receptors provide insight into its axon guidance mechanism, Science 344, 1275-1279.
June 5, 2014
King, N. P., Bale, J. B., Sheffler, W., McNamara, D. E., Gonen, S., Gonen, T., Yeates, T. O., and Baker, D. (2014) Accurate design of co-assembling multi-component protein nanomaterials, Nature 510, 103-108.
May 22, 2014
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