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.
August 2, 2016
Jain, R., Coloma, J., Garcia-Sastre, A., and Aggarwal, A. K. (2016) Structure of the NS3 helicase from Zika virus, Nat. Struct. Mol. Biol. [Epub ahead of print]
June 21, 2016
Yao, G., Zhang, S., Mahrhold, S., Lam, K. H., Stern, D., Bagramyan, K., Perry, K., Kalkum, M., Rummel, A., Dong, M., and Jin, R. (2016) N-Linked Glycosylation of Sv2 Is Required for Binding and Uptake of Botulinum Neurotoxin A, Nat. Struct. Mol. Biol. 23, 656-662.
May 26, 2016
Chung, B. C., Mashalidis, E. H., Tanino, T., Kim, M., Matsuda, A., Hong, J., Ichikawa, S., and Lee, S. Y. (2016) Structural insights into inhibition of lipid I production in bacterial cell wall synthesis, Nature 533, 557-5690.
April 28, 2016
Schmidt, H. R., Zheng, S., Gurpinar, E., Koehl, A., Manglik, A., and Kruse, A. C. (2016) Crystal structure of the human σ1 receptor, Nature 532, 527-530.
April 21, 2016
Coleman, J. A., Green, E. M., and Gouaux, E. (2016) X-ray structures and mechanism of the human serotonin transporter, Nature 532, 334-339.
March 17, 2016
Li, L., Park, E., Ling, J., Ingram, J., Ploegh, H., and Rapoport, T. A. (2016) Crystal structure of a substrate-engaged SecY protein-translocation channel, Nature 531, 395-399.
February 25, 2016
Hayes, R. P., Xiao, Y., Ding, F., van Erp, P. B. G., Rajashankar, K., Bailey, S., Wiedenheft, B., and Ke, A. (2016) Structural basis for promiscuous PAM recognition in type I–E Cascade from E. coli, Nature 530, 499-503. PMID: 26863189.
February 18, 2016
Yin, Z., Shi, K., Banerjee, S., Pandey, K. K., Bera, S., Grandgenett, D. P., and Aihara, H. (2016) Crystal structure of the Rous sarcoma virus intasome, Nature 530, 362-366. PMID: 26887497.
February 5, 2016
Petrou, V. I., Herrera, C. M., Schultz, K. M., Clarke, O. B., Vendome, J., Tomasek, D., Banerjee, S., Rajashankar, K. R., Belcher Dufrisne, M., Kloss, B., Kloppmann, E., Rost, B., Klug, C. S., Trent, M. S., Shapiro, L., and Mancia, F. (2016) Structures of aminoarabinose transferase ArnT suggest a molecular basis for lipid A glycosylation, Science 351, 608-612.
January 1, 2016
Saxton, R. A., Knockenhauer, K. E., Wolfson, R. L., Chantranupong, L., Pacold, M. E., Wang, T., Schwartz, T. U., and Sabatini, D. M. (2016) Structural basis for leucine sensing by the Sestrin2-mTORC1 pathway, Science 351, 53-58.
November 12, 2015
Tao, Y., Cheung, L. S., Li, S., Eom, J.-S., Chen, L.-Q., Xu, Y., Perry, K., Frommer, W. B., and Feng, L. (2015) Structure of a eukaryotic SWEET transporter in a homotrimeric complex, Nature 527, 259-263.
October 30, 2015
Jiang, J., Chan, H., Cash, D. D., Miracco, E. J., Ogorzalek Loo, R. R., Upton, H. E., Cascio, D., O'Brien Johnson, R., Collins, K., Loo, J. A., Zhou, Z. H., and Feigon, J. (2015) Structure of Tetrahymena telomerase reveals previously unknown subunits, functions, and interactions, Science 350, aab4070.
October 29, 2015
Wei, J., and Tong, L. (2015) Crystal structure of the 500-kDa yeast acetyl-CoA carboxylase holoenzyme dimer, Nature 526, 723-727.
October 22, 2015
Rubinstein, R., Thu, C. A., Goodman, K. M., Wolcott, H. N., Bahna, F., Mannepalli, S., Ahlsen, G., Chevee, M., Halim, A., Clausen, H., Maniatis, T., Shapiro, L., and Honig, B. (2015) Molecular Logic of Neuronal Self-Recognition through Protocadherin Domain Interactions, Cell 163, 629-642.
Jost, M., Fernandez-Zapata, J., Polanco, M. C., Ortiz-Guerrero, J. M., Chen, P. Y., Kang, G., Padmanabhan, S., Elias-Arnanz, M., and Drennan, C. L. (2015) Structural basis for gene regulation by a B12-dependent photoreceptor, Nature 526, 536–541. PMID: 26416754. 24-ID-C; Pilatus
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