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OverviewThe 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.
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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. |
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