Determination of Ligand-Kinase Crystal Structures

Experiments involving target-drug complex formation, data collection, and data processing were done using the standard operating protocol as validated previously^{6 (link)} for the determination of atomic resolution ligand–kinase crystal structures. Protein purification^{6 (link)} was done using a combination of affinity-based adsorption chromatography (HisTrap™; GE Healthcare), gel filtration (HiPrep 26/10 column; GE Healthcare) and ion exchange chromatography (Q Sepharose™; GE Healthcare).

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Roy S.M., Grum-Tokars V.L., Schavocky J.P., Saeed F., Staniszewski A., Teich A.F., Arancio O., Bachstetter A.D., Webster S.J., Van Eldik L.J., Minasov G., Anderson W.F., Pelletier J.C, & Watterson D.M. (2015). Targeting Human Central Nervous System Protein Kinases: An Isoform Selective p38αMAPK Inhibitor That Attenuates Disease Progression in Alzheimer’s Disease Mouse Models. ACS Chemical Neuroscience, 6(4), 666-680.

Publication 2015

HisTrap™; HiPrep 26/10 column Q Sepharose™;

Adsorption Affinity chromatography Gel filtration Ion exchange chromatography Kinase Ligand Protein Sepharose Target drug

Corresponding Organization :

Other organizations : Northwestern University, Columbia University, University of Kentucky

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Variable analysis

independent variables

Target-drug complex formation

dependent variables

Atomic resolution ligand–kinase crystal structures

control variables

Protein purification using a combination of affinity-based adsorption chromatography (HisTrap™; GE Healthcare), gel filtration (HiPrep 26/10 column; GE Healthcare) and ion exchange chromatography (Q Sepharose™; GE Healthcare)

controls

Positive controls and negative controls not explicitly mentioned.

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