Solving a three-dimensional structure of a biomacromolecule using X-ray crystallographic techniques Is a mulfi-step process and one ofthe major bottlenecks is obtaining a highly pure (>95%) and homogeneous (non-aggregated) protein sample. The goal In establishing a Protein Production Core facility Is to assist Invesfigators In expressing and purifying their proteln(s) of Interest in high yield, purity, and homogeneity. The proposed PPC will be equipped with modern equipment for growth of bacteria, yeast, and insect cells for expression of recombinant proteins. It will also house automated equipment for liquid column chromatography (FPLC) and analysis (electrophoresis). Users ofthe facility will be trained on the equipment by a staff manager. The PPC manager will oversee all maintenance and operafion ofthe facility and, in consultafion with the Core Director, will also have fiscal responsibility of ensuring that a reasonable costrecovery system is established in consultation with the PI, lAC and EAC. The PPC facility will be housed in the new Stephenson Life Sciences Research Center immediately adjacent to the OU X-ray core facility. The PPC wlll enhance overall productivity of not only COBRE and OSBN investigators but also the larger molecular biosciences community at the University of Oklahoma and other Institufions statewide.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Exploratory Grants (P20)
Project #
5P20GM103640-03
Application #
8666003
Study Section
Special Emphasis Panel (ZRR1-RI-B)
Project Start
Project End
Budget Start
2014-06-01
Budget End
2015-05-31
Support Year
3
Fiscal Year
2014
Total Cost
$188,159
Indirect Cost
$62,720
Name
University of Oklahoma Norman
Department
Type
DUNS #
848348348
City
Norman
State
OK
Country
United States
Zip Code
73019
Hebdon, Skyler D; Menon, Smita K; Richter-Addo, George B et al. (2018) Regulatory Targets of the Response Regulator RR_1586 from Clostridioides difficile Identified Using a Bacterial One-Hybrid Screen. J Bacteriol 200:
Cruz-Reyes, Jorge; Mooers, Blaine H M; Doharey, Pawan K et al. (2018) Dynamic RNA holo-editosomes with subcomplex variants: Insights into the control of trypanosome editing. Wiley Interdiscip Rev RNA 9:e1502
Booe, Jason M; Warner, Margaret L; Roehrkasse, Amanda M et al. (2018) Probing the Mechanism of Receptor Activity-Modifying Protein Modulation of GPCR Ligand Selectivity through Rational Design of Potent Adrenomedullin and Calcitonin Gene-Related Peptide Antagonists. Mol Pharmacol 93:355-367
Muthuramalingam, Meenakumari; White, John C; Murphy, Tamiko et al. (2018) The toxin from a ParDE toxin-antitoxin system found in Pseudomonas aeruginosa offers protection to cells challenged with anti-gyrase antibiotics. Mol Microbiol :
Roehrkasse, Amanda M; Booe, Jason M; Lee, Sang-Min et al. (2018) Structure-function analyses reveal a triple ?-turn receptor-bound conformation of adrenomedullin 2/intermedin and enable peptide antagonist design. J Biol Chem 293:15840-15854
Vazquez Reyes, Carolina; Tangprasertchai, Narin S; Yogesha, S D et al. (2017) Nucleic Acid-Dependent Conformational Changes in CRISPR-Cas9 Revealed by Site-Directed Spin Labeling. Cell Biochem Biophys 75:203-210
Van Orden, Mason J; Klein, Peter; Babu, Kesavan et al. (2017) Conserved DNA motifs in the type II-A CRISPR leader region. PeerJ 5:e3161
Murugan, Karthik; Babu, Kesavan; Sundaresan, Ramya et al. (2017) The Revolution Continues: Newly Discovered Systems Expand the CRISPR-Cas Toolkit. Mol Cell 68:15-25
Li, Yangxiong; Lavey, Nathan P; Coker, Jesse A et al. (2017) Consequences of Depsipeptide Substitution on the ClpP Activation Activity of Antibacterial Acyldepsipeptides. ACS Med Chem Lett 8:1171-1176
Wang, Bing; Powell, Samantha M; Guan, Ye et al. (2017) Nitrosoamphetamine binding to myoglobin and hemoglobin: Crystal structure of the H64A myoglobin-nitrosoamphetamine adduct. Nitric Oxide 67:26-29

Showing the most recent 10 out of 47 publications