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. 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 #
5P20RR017708-05
Application #
7381951
Study Section
Special Emphasis Panel (ZRR1-RI-A (03))
Project Start
2006-07-01
Project End
2007-06-30
Budget Start
2006-07-01
Budget End
2007-06-30
Support Year
5
Fiscal Year
2006
Total Cost
$169,319
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
McNiff, M L; Haynes, E P; Dixit, N et al. (2016) Thioredoxin fusion construct enables high-yield production of soluble, active matrix metalloproteinase-8 (MMP-8) in Escherichia coli. Protein Expr Purif 122:64-71
Johnson, Troy A; Mcleod, Matthew J; Holyoak, Todd (2016) Utilization of Substrate Intrinsic Binding Energy for Conformational Change and Catalytic Function in Phosphoenolpyruvate Carboxykinase. Biochemistry 55:575-87
Tucker, Jenifer K; McNiff, Michaela L; Ulapane, Sasanka B et al. (2016) Mechanistic investigations of matrix metalloproteinase-8 inhibition by metal abstraction peptide. Biointerphases 11:021006
Yadav, Rahul; Vattepu, Ravi; Beck, Moriah R (2016) Phosphoinositide Binding Inhibits Actin Crosslinking and Polymerization by Palladin. J Mol Biol 428:4031-4047
Gurung, Ritu; Yadav, Rahul; Brungardt, Joseph G et al. (2016) Actin polymerization is stimulated by actin cross-linking protein palladin. Biochem J 473:383-96

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