Here we present initial NMR Spectroscopic studies of CrgA, one of the important putative inner membrane proteins in Mycobacterium tuberculosis (Mtb). CrgA helps in the cell division of Mtb contains 2 transmembrane helices (TM), 93 amino acid and is an important drug target. Our studies show that, CrgA interacts with FtsZ (involves in Zring formation during cell division) and Rv0008c (another putative membrane protein) in Mtb during the cell division. For NMR structural studies 15N, 13C uniform and amino acid specific isotope labeled CrgA reconstituted in POPC-POPG (4:1 mol/mol) liposomes was used for planar lipid bilayer oriented on glass slides and Magic Angle Spinning (MAS) correlation spectroscopy. The key behind these studies is to determine CrgA structure in membrane mimetic lipid bilayer environment. For oriented glass slide samples, 2D PISEMA experiments were performed which correlates 1H-15N dipolar coupling with the 15N chemical shift from the backbone resonances of 15N labeled protein in lipid bilayer. Each measured frequency reflects the orientation of the peptide plane of the protein w.r.t to the bilayer normal. Similarly the tilt angles of various parts of the protein (TM, N and C terminal) can also be obtained which is very useful for the structure calculation process. Moreover MAS experiments can measure distances between side chains of various residues. Altogether the aim of this research is to characterize the 3D backbone as well as the side chain structures of CrgA in native membrane like environment.