This subproject is one of many research subprojects utilizing theresources provided by a Center grant funded by NIH/NCRR. The subproject andinvestigator (PI) may have received primary funding from another NIH source,and thus could be represented in other CRISP entries. The institution listed isfor the Center, which is not necessarily the institution for the investigator.X-ray crystallography is the most powerful tool in the determination of the three-dimensional structure of proteins, and in the elucidation of their structure-function relationships and their interactions with other macromolecules as well as small molecule ligands including drugs. The major aim of Core B is to establish, equip and staff with an experienced Director a Protein Structure Laboratory (PSL) built around state-of-the-art x-ray crystallography instrumentation to support the research community of the state of Kansas. Our facilities include a high brilliance RUH3R X-ray generator, Raxis IV++ imaging plate and an Xtream 2000 cryocooling system. We currently provide access of X-ray beam to a number of crystallographers. We also provide crystallographers and non-crystallographers services involving protein crystallization, X-ray diffraction data collection, phase determination, model building and crystallographic refinement, as well as help with grant application and writing publications.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Exploratory Grants (P20)
Project #
2P20RR017708-06A1
Application #
7720667
Study Section
National Center for Research Resources Initial Review Group (RIRG)
Project Start
2008-05-15
Project End
2009-03-31
Budget Start
2008-05-15
Budget End
2009-03-31
Support Year
6
Fiscal Year
2008
Total Cost
$162,015
Indirect Cost
Name
University of Kansas Lawrence
Department
Pharmacology
Type
Schools of Pharmacy
DUNS #
076248616
City
Lawrence
State
KS
Country
United States
Zip Code
66045
Garabedian, Alyssa; Baird, Matthew A; Porter, Jacob et al. (2018) Linear and Differential Ion Mobility Separations of Middle-Down Proteoforms. Anal Chem 90:2918-2925
Jeanne Dit Fouque, Kevin; Garabedian, Alyssa; Porter, Jacob et al. (2017) Fast and Effective Ion Mobility-Mass Spectrometry Separation of d-Amino-Acid-Containing Peptides. Anal Chem 89:11787-11794
Alaofi, Ahmed; Farokhi, Elinaz; Prasasty, Vivitri D et al. (2017) Probing the interaction between cHAVc3 peptide and the EC1 domain of E-cadherin using NMR and molecular dynamics simulations. J Biomol Struct Dyn 35:92-104
Pang, Xiao-Yan; Wang, Suya; Jurczak, Michael J et al. (2017) Retinol saturase modulates lipid metabolism and the production of reactive oxygen species. Arch Biochem Biophys 633:93-102
McNiff, Michaela L; Chadwick, Jennifer S (2017) Metal-bound claMP Tag inhibits proteolytic cleavage. Protein Eng Des Sel 30:467-475
Gowthaman, Ragul; Miller, Sven A; Rogers, Steven et al. (2016) DARC: Mapping Surface Topography by Ray-Casting for Effective Virtual Screening at Protein Interaction Sites. J Med Chem 59:4152-70
Kumar, Ritesh; Qi, Yifei; Matsumura, Hirotoshi et al. (2016) Replacing Arginine 33 for Alanine in the Hemophore HasA from Pseudomonas aeruginosa Causes Closure of the H32 Loop in the Apo-Protein. Biochemistry 55:2622-31
Meekins, David A; Zhang, Xin; Battaile, Kevin P et al. (2016) 1.45?Å resolution structure of SRPN18 from the malaria vector Anopheles gambiae. Acta Crystallogr F Struct Biol Commun 72:853-862
Damalanka, Vishnu C; Kim, Yunjeong; Alliston, Kevin R et al. (2016) Oxadiazole-Based Cell Permeable Macrocyclic Transition State Inhibitors of Norovirus 3CL Protease. J Med Chem 59:1899-913
Wahome, Newton; Sully, Erin; Singer, Christopher et al. (2016) Novel Ricin Subunit Antigens With Enhanced Capacity to Elicit Toxin-Neutralizing Antibody Responses in Mice. J Pharm Sci 105:1603-1613

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