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
NE-CAT maintains a chemistry laboratory for use by its resident staff members and beam line users adjacent to the Sector 24-ID beam lines. The laboratory is fully equipped for protein crystallization and crystal soaking experiments. Chemicals normally used are readily available as well as routine chemical equipment such as analytical balances, a pH meter, an ultrasound dismembrator, a table-top refrigerated shaker, a high-speed refrigerated Ependorf centrifuge, a UV/Vis spectrophotometer, and two high-power stereo zoom microscopes. In addition, there is a Agilent 2100 Bioanalyzer available for fast and precise characterization of molecular weights and concentrations of proteins and DNA, a dynamic light scattering apparatus which can be used to provide unique insights into the behavior of biomolecules in solution by measuring the hydrodynamic radius and polydisersity of macromolecules, and an AKTA/FPLC system housed in a temperature controlled 4 degree Centigrade box for high- throughput automated analytical and preparative protein purification. Two temperature controlled incubators are available, at 4 and 18 degrees Centigrade. There is also a small -35 degree Centigrade refrigerator available for storage of samples as well as a 9x 10 foot walk in cold room maintained at 4 degrees Centigrade.
Marcia, M., and Pyle, A.M. (2012)
Baconguis, I., and Gouaux, E. (2012) Structural plasticity and dynamic selectivity of acid-sensing ion channel-spider toxin complexes, Nature 489, 400-405.
Nakanishi, K., Weinberg, D. E., Bartel, D. P., and Patel, D. J. (2012) Structure of yeast Argonaute with guide RNA, Nature 486, 368-374.
Sosa, 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.
Hattori, M., and Gouaux, E. (2012) Molecular mechanism of ATP binding and ion channel activation in P2X receptors, Nature 485, 207-212.
Polikanov, 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.
Kung, 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.
Laganowsky, 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.
Brohawn, 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.
Scott, 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.
Hu, J., Xue, Y., Lee, S., and Ha, Y. (2011) The crystal structure of GXGD membrane protease FlaK, Nature 475, 528-531
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