: MacCHESS, a synchrotron radiation Research Resource for macromolecular crystallography, has the overall goal of advancing the frontiers of structural biology through innovative technical research and development and user support. MacCHESS leverages the National Science Foundation investments in the Cornell High Energy Synchrotron Source (CHESS), which maintains the synchrotron radiation laboratory, and the Laboratory for Elementary Particle Physics (LEPP), which operates the storage ring. MacCHESS technical developments are driven by both core and collaborative research projects involving a broad range of macromolecules. In addition to performing technical R&D and core research, MacCHESS provides specialized instrumentation for macromolecular crystallography and a staff for user training and support. MacCHESS has established itself as one of the most productive facilities in the world for macromolecular crystallography with almost 400 papers published during the past four years as a result of MacCHESS related technical research and development, core and collaborative research and service. More than 23 of these papers were published in the high visibility journals, Science, Nature, and Cell. Three CHESS stations, A-1, F-1 and F-2, are used for macromolecular crystallography experiments. During the next five years, MacCHESS technical R&D will focus on (1) microcrystallography, (2) pressure crycooling and related procedures, (3) SAXS and envelope phasing, (4) automation and high-throughput, and (5) a new station for long wavelength crystallography. Each of these technical R&D efforts is driven by the challenging problems presented by collaborating investigators who study the atomic structure of molecules and complexes of great current interest to medicine and biology, including membrane proteins, signaling protein complexes, nucleic acid/protein complexes, protein drug interactions and viruses. Technical developments resulting from MacCHESS research are freely available to the scientific community and disseminated through meetings, workshops, publications, web distributions and collaborations with other synchrotron sources.

National Institute of Health (NIH)
National Center for Research Resources (NCRR)
Biotechnology Resource Grants (P41)
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Special Emphasis Panel (ZRG1-BCMB-E (40))
Program Officer
Swain, Amy L
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Cornell University
Schools of Arts and Sciences
United States
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Kozlov, Guennadi; Wong, Kathy; Gehring, Kalle (2018) Crystal structure of the Legionella effector Lem22. Proteins 86:263-267
Ménade, Marie; Kozlov, Guennadi; Trempe, Jean-François et al. (2018) Structures of ubiquitin-like (Ubl) and Hsp90-like domains of sacsin provide insight into pathological mutations. J Biol Chem 293:12832-12842
Xu, Jie; Kozlov, Guennadi; McPherson, Peter S et al. (2018) A PH-like domain of the Rab12 guanine nucleotide exchange factor DENND3 binds actin and is required for autophagy. J Biol Chem 293:4566-4574
Dean, Dexter N; Rana, Pratip; Campbell, Ryan P et al. (2018) Propagation of an A? Dodecamer Strain Involves a Three-Step Mechanism and a Key Intermediate. Biophys J 114:539-549
Chen, Yu Seby; Kozlov, Guennadi; Fakih, Rayan et al. (2018) The cyclic nucleotide-binding homology domain of the integral membrane protein CNNM mediates dimerization and is required for Mg2+ efflux activity. J Biol Chem 293:19998-20007
Xu, Caishuang; Kozlov, Guennadi; Wong, Kathy et al. (2016) Crystal Structure of the Salmonella Typhimurium Effector GtgE. PLoS One 11:e0166643
Cogliati, Massimo; Zani, Alberto; Rickerts, Volker et al. (2016) Multilocus sequence typing analysis reveals that Cryptococcus neoformans var. neoformans is a recombinant population. Fungal Genet Biol 87:22-9
Oot, Rebecca A; Kane, Patricia M; Berry, Edward A et al. (2016) Crystal structure of yeast V1-ATPase in the autoinhibited state. EMBO J 35:1694-706
Lucido, Michael J; Orlando, Benjamin J; Vecchio, Alex J et al. (2016) Crystal Structure of Aspirin-Acetylated Human Cyclooxygenase-2: Insight into the Formation of Products with Reversed Stereochemistry. Biochemistry 55:1226-38
Bauman, Joseph D; Harrison, Jerry Joe E K; Arnold, Eddy (2016) Rapid experimental SAD phasing and hot-spot identification with halogenated fragments. IUCrJ 3:51-60

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