Abstract
We describe here the expression, purification, solid state NMR sample preparation, and initial structural and functional data for three membrane proteins from Mycobacterium tuberculosis (Mtb). The three proteins are FtsX, Rv0008c and Rv1861. Solid state NMR is uniquely able to characterize protein structure in a liquid crystalline lipid bilayer environment. We have used N terminal His tag for protein purification. Nickel-NTA chromatography was performed using a semi automated FPLC instrument. Purified 15N labeled proteins were eluted into 0.2% (Rv0008c and Rv1861) and 0.4% (FtsX) solution of dodecylphosphocholine (DPC) detergent.
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