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
Mooers, Blaine H M (2016) Simplifying and enhancing the use of PyMOL with horizontal scripts. Protein Sci 25:1873-82
Cruz-Reyes, Jorge; Mooers, Blaine H M; Abu-Adas, Zakaria et al. (2016) DEAH-RHA helicase•Znf cofactor systems in kinetoplastid RNA editing and evolutionarily distant RNA processes. RNA Dis 3:
Isom, Catherine E; Menon, Smita K; Thomas, Leonard M et al. (2016) Crystal structure and DNA binding activity of a PadR family transcription regulator from hypervirulent Clostridium difficile R20291. BMC Microbiol 16:231
Lavey, Nathan P; Coker, Jesse A; Ruben, Eliza A et al. (2016) Sclerotiamide: The First Non-Peptide-Based Natural Product Activator of Bacterial Caseinolytic Protease P. J Nat Prod 79:1193-7
Vazquez Reyes, Carolina; Tangprasertchai, Narin S; Yogesha, S D et al. (2016) Nucleic Acid-Dependent Conformational Changes in CRISPR-Cas9 Revealed by Site-Directed Spin Labeling. Cell Biochem Biophys :
Wang, Bing; Powell, Samantha M; Hessami, Neda et al. (2016) Crystal structures of two nitroreductases from hypervirulent Clostridium difficile and functionally related interactions with the antibiotic metronidazole. Nitric Oxide 60:32-39
Mooers, Blaine H M (2016) Direct-methods structure determination of a trypanosome RNA-editing substrate fragment with translational pseudosymmetry. Acta Crystallogr D Struct Biol 72:477-87
Wang, Bing; Thomas, Leonard M; Richter-Addo, George B (2016) Organometallic myoglobins: Formation of Fe-carbon bonds and distal pocket effects on aryl ligand conformations. J Inorg Biochem 164:1-4
Kumar, Vikas; Madina, Bhaskara R; Gulati, Shelly et al. (2016) REH2C Helicase and GRBC Subcomplexes May Base Pair through mRNA and Small Guide RNA in Kinetoplastid Editosomes. J Biol Chem 291:5753-64
Madina, Bhaskara R; Kumar, Vikas; Mooers, Blaine H M et al. (2015) Native Variants of the MRB1 Complex Exhibit Specialized Functions in Kinetoplastid RNA Editing. PLoS One 10:e0123441

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