This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The primary focus of this initiative is to upgrade the CHESS F3 bend-magnet station to be a flexible, double-focused, high-intensity X-ray beamline for long wavelength protein crystallography, including SAD and microcrystal studies. Key to the new capabilities will be a flexible optics system that can accommodate a user-selectable choice of narrow energy-bandpass synthetic multilayer mirrors and focusing elements to optimize particular data collection requirements. Long wavelength, lower energy X-ray capabilities are not commonly available at synchrotron radiation sources today because most beamlines have been designed to deliver high flux. The best high-flux X-ray sources utilize insertion devices, wigglers or undulators, as their X-ray sources. Insertion devices do produce high X-ray intensities but they also produce high heat loads at the same time. To handle these heat loads, beamlines are designed with vacuum windows and graphite filters to dissipate the heat and protect storage ring ultra-high vacuum environments. The windows, however, absorb the long wavelength light and make it virtually impossible to collect high-flux, high signal-to-noise data at wavelengths below 8 keV (1. 5 ?). Our collaborators have shown tremendous interest in utilizing a powerful beamline at long wavelengths. 1) The Cingolani group (SUNY Upstate Medical University) deals with the mechanisms of

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001646-28
Application #
8171512
Study Section
Special Emphasis Panel (ZRG1-BCMB-E (40))
Project Start
2010-07-01
Project End
2011-06-30
Budget Start
2010-07-01
Budget End
2011-06-30
Support Year
28
Fiscal Year
2010
Total Cost
$61,764
Indirect Cost
Name
Cornell University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
872612445
City
Ithaca
State
NY
Country
United States
Zip Code
14850
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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