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. The approximate protein yield were 45mg/l (Rv0008c), 50mg/l (FtsX) and 25mg/l (Rv1861) respectively. Samples for solid state NMR were prepared by removing the detergent from the purified protein by exhaustive dialysis against 10mM Tris-HCl (pH-8.0) coincident with reconstitution into lipid bilayers. To prepare aligned samples, pelleted liposomes were layered on to thin glass slides and stacked. 30-35 glass slides were hydrated in a process called ‘wet stacking’followed by sealing them into a rectangular glass cell. 400 and 600 MHz magnets were used to determine the 1D and 2D spectra of these aligned samples such that the bilayer is parallel to the applied magnetic field direction. FtsX is an ABC transporter containing 4 transmembrane helices (TMH) and its interaction with FtsZ participate in cell division. Rv1861 has 3 TMH and is known to hydrolyze ATP. It forms a stable octameric structure that is presumably facilitated by the GxxxG, GxxxA, and AxxxA sequences in the trasmembrane stretches. Rv0008c is a Mtb membrane protein and participates in cell division. It has been found previously in our laboratory that Rv0008c interacts with Rv0011c and this interaction along with other membrane proteins can facilitate the Mtb cell division process.