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
Status of NE-CAT Sector 24 Activities
The accelerator was shut down for scheduled preventative maintenance for nearly the entire month of May. These long accelerator shutdown periods, which occur three times a year, are used by the NE- CAT staff to perform their own preventative maintenance on the beamlines and to install and test new capabilities for its users.
The major emphasis during this shutdown period was to develop a new software interface between the Console beamline control system and the MD2 microdiffractometer control system. When delivered, the MD2 was supplied with its own control system and Maatel had also provided an interface to enable the MD2 to communicate with an external control system. However in usage, our users would periodically experience a hang up requiring rebooting of the system due to problems with the supplied interface. Also the communications between the Console control system and the MD2 software through the supplied interface were very slow, appreciably slowing down the automated sample placement robot operation as well as the rate at which data frames could be taken. To alleviate this problem, a new interface software system was developed and installed during the shutdown period. Following resumption of APS accelerator operations on May 27, our staff thoroughly tested the new interface before arrival of the first users. The new interface was found to be highly reliable; totally eliminating the hang up problems previously encountered and permitted must faster operations. The complete cycle of pin dismount and new pin remount on the goniometer using the sample placement robot was decreased from 2-1/2 minutes to 1-1/4 minutes. Also, the rate at which data frames could be taken was increased by a factor of two. Based upon the successful testing of the new interface, this new control interface has now been installed on both beamlines for routine operations.
Several other new features have been added. A triple aperture assembly has been purchased from ACCEL/Maatel. This assembly contains three different sized apertures. From the control area users can now automatically select which of the three aperture sizes they wish to use- avoiding the need to go in and out of the experimental hutch to manually change apertures. A MD2 Kappa attachment for the MD2 is now available for routine use by our users on the 24-ID-C beamline. To facilitate use of the Kappa, we have made available to the users the STAC (Strategy for Aligned Crystals) software. STAC allows the user to automatically determine the correct orientation of the crystal and provides an optimum data acquisition strategy to be used.
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.
Read the article.
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.
Read the article.
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
© 2005 Northeastern Collaborative Access Team
Webmaster: Cyndi Salbego