Abstract
Multimilligram quantities of active and pure GluR2-S1S2, the recombinant ligand binding core of the AMPA-sensitive GluR2 receptor, were produced by preparative folding of the solubilized inclusion bodies expressed in 1 l of Escherichia coli cell culture. The biochemical properties and biological activities of folded protein were characterized and the protein construct was optimized for three-dimensional structural studies.
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