The main goal of the NE-CAT Resource is to provide user access to state-of-the-art synchrotron beamlines for macromolecular crystallography. NE-CAT began planning and design for two beamlines in 2001. Beamline 24- ID-C became available to the Advanced Photon Source users in 2006 and beamline 24-ID-E became available in 2007. During the ensuing years, beamline improvements have resulted in ultrastable, small X-ray beams ideally suited for challenging problems in macromolecular crystallography. Each beamline is equipped with a high capacity sample automounter and a microdiffractometer. Beamline 24-ID-C features a PILATUS 6MF pixel array detector, and by early 2017 an EIGER 16M pixel array detector will be available on beamline ID-24- E. NE-CAT provides automated software for data collection and analysis (RAPD) and a Web-based interface for remote data collection. We will continue to provide routine maintenance to ensure efficient and reliable data collection, and we propose an upgrade program to maintain state-of-the-art capabilities over the five years covered by this application. NE-CAT has an experienced and dedicated scientific staff who enable access to the beamlines. The staff is available or on call 24/7 to assist users with data collection and processing needs. This highly regarded staff is a major strength of NE-CAT. NE-CAT has an outstanding record of reliability with technical problems rarely interfering with user access. NE-CAT is directed by Dr. Steven Ealick, who has more that 25 years of experience overseeing the operation of synchrotron facilities for macromolecular crystallography. The technical group, led by Deputy Director Dr. Malcolm Capel, and the operations group, led by Associate Director Dr. Kanagalaghatta Rajashankar work closely together to ensure that the needs of the user community are met. Assistant Director Dr. Frank Murphy is responsible for development and maintenance of RAPD. Together, these four individuals make up the NE-CAT management team. NE-CAT beam time is in high demand, and each run all available beamtime is allocated to users. NE-CAT typically hosts more than 1500 users per year from about 160 unique user groups, either on site or remotely. NE-CAT users published about 150 papers during the last year, and they are projected to publish around 170 in 2016. NE-CAT's record of productivity places us among the top of worldwide facilities for macromolecular crystallography. NE-CAT operates an extensive user training program adaptable to first time users, advanced users with technically challenging problems, and everyone in between. A Web site is available to provide all information needed by new or current users. NE-CAT participates in many training and outreach activities including organization of an annual workshop and participation in professional society meetings. The staff works closely with user groups and are often invited to coauthor manuscripts resulting from user assistance.
The purpose of the proposed Resource is to provide the biomedical community with access to state-of- the-art facilities for macromolecular crystallography. The Resource will enhance our ability to visualize the three-dimensional structures of biological macromolecules. Many of these molecules are targets for drug design, and understanding their structures will aid in the development of new pharmaceutical agents. In addition, these structures allow us to better understand basic biological systems often resulting in the identification of new pharmaceutical targets.
|Jenson, Justin M; Xue, Vincent; Stretz, Lindsey et al. (2018) Peptide design by optimization on a data-parameterized protein interaction landscape. Proc Natl Acad Sci U S A 115:E10342-E10351|
|De-la-Torre, Pedro; Choudhary, Deepanshu; Araya-Secchi, Raul et al. (2018) A Mechanically Weak Extracellular Membrane-Adjacent Domain Induces Dimerization of Protocadherin-15. Biophys J 115:2368-2385|
|Merz, Gregory E; Borbat, Peter P; Muok, Alise R et al. (2018) Site-Specific Incorporation of a Cu2+ Spin Label into Proteins for Measuring Distances by Pulsed Dipolar Electron Spin Resonance Spectroscopy. J Phys Chem B 122:9443-9451|
|Shi, Ke; Carpenter, Michael A; Banerjee, Surajit et al. (2017) Structural basis for targeted DNA cytosine deamination and mutagenesis by APOBEC3A and APOBEC3B. Nat Struct Mol Biol 24:131-139|
|Yao, Guorui; Lam, Kwok-Ho; Perry, Kay et al. (2017) Crystal Structure of the Receptor-Binding Domain of Botulinum Neurotoxin Type HA, Also Known as Type FA or H. Toxins (Basel) 9:|
|Crochet, Robert B; Kim, Jeong-Do; Lee, Herie et al. (2017) Crystal structure of heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB2) and the inhibitory influence of citrate on substrate binding. Proteins 85:117-124|
|Gulati, Sahil; Jastrzebska, Beata; Banerjee, Surajit et al. (2017) Photocyclic behavior of rhodopsin induced by an atypical isomerization mechanism. Proc Natl Acad Sci U S A 114:E2608-E2615|
|Yao, Guorui; Lam, Kwok-Ho; Weisemann, Jasmin et al. (2017) A camelid single-domain antibody neutralizes botulinum neurotoxin A by blocking host receptor binding. Sci Rep 7:7438|
|Silvaroli, Josie A; Pleshinger, Matthew J; Banerjee, Surajit et al. (2017) Enzyme That Makes You Cry-Crystal Structure of Lachrymatory Factor Synthase from Allium cepa. ACS Chem Biol 12:2296-2304|
|Su, Chih-Chia; Yin, Linxiang; Kumar, Nitin et al. (2017) Structures and transport dynamics of a Campylobacter jejuni multidrug efflux pump. Nat Commun 8:171|
Showing the most recent 10 out of 13 publications