Abstract

Solving a three-dimensional structure of a biomacromolecule using X-ray crystallographic techniques Is a multi-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 Investigators In expressing and purifying their protein(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 operation ofthe facility and, in consultation with the Core Director, will also have fiscal responsibility of ensuring that a reasonable cost recovery 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 will enhance overall productivity of not only COBRE and OSBN investigators but also the larger molecular biosciences community at the University of Oklahoma and other Institutions statewide.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Exploratory Grants (P20)
Project #
5P20GM103640-02
Application #
8518424
Study Section
Special Emphasis Panel (ZRR1-RI-B)
Project Start
Project End
Budget Start
2013-06-01
Budget End
2014-05-31
Support Year
2
Fiscal Year
2013
Total Cost
$181,574
Indirect Cost
$60,525

  Institution

Name
University of Oklahoma Norman
Department
Type
DUNS #
848348348
City
Norman
State
OK
Country
United States
Zip Code
73019

  Publications

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
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
Sundaresan, Ramya; Parameshwaran, Hari Priya; Yogesha, S D et al. (2017) RNA-Independent DNA Cleavage Activities of Cas9 and Cas12a. Cell Rep 21:3728-3739

Showing the most recent 10 out of 47 publications