Mycobacterium tuberculosis is known to have a very thick and hydrophobic outer membrane, due to richness in long hydrophobic mycolic acids.Nutrition and waste transportation across M.tuberculosis membrane was very slow.So far, only three outer membrane channels were connotated in M.tuberculosis, comparing over 60 outer membrane proteins in E.coli.Two M.tuberculosis outer membrane proteins were over-expressed in E.coli and purified in the presence of detergent micelles for structural studies.X-ray crystallography and solution NMR were applied to determine structures of the two proteins and resulted in high resolution.Structure analysis of the proteins illustrate that there is no presence of hydrophilic pore region in these two outer-membrane proteins, which is very much contradiction to their biochemical, and channel conductance electro-physiological data.More collaborations efforts between microbiology physiology and structural studies are laid to reconcile the obvious discrepancies.