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.
December 13, 2017
Born, D. A., Ulrich, E. C., Ju, K. S., Peck, S. C., van der Donk, W. A., and Drennan, C. L. (2017) Structural basis for methylphosphonate biosynthesis, Science 358, 1336-1339.
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November 27, 2017
October 5, 2017
Xiao, Y., Ng, S., Nam, K. H., and Ke, A. (2017) How type II CRISPR-Cas establish immunity through Cas1-Cas2-mediated spacer integration, Nature 550, 137-141.
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September 21, 2017
Hinshaw, S. M., Makrantoni, V., Harrison, S. C., and Marston, A. L. (2017) The Kinetochore Receptor for the Cohesin Loading Complex, Cell 171, 72-84
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 548, 420-425.
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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