Gram-negative bacteria cause multiple infectious disease and are increasingly becoming resistant to antibiotics. However, development of drugs targeting these organisms is complicated by the extreme complexity of the structure of gram-negative cell wall. In research recently published in Nature (Nature, 2017) Dr. Maofu Liao from the Department of Cell Biology at Harvard Medical School used high-resolution single-particle cryo-electron microscopy to elucidate the structure of an essential bacterial ABC (ATP-binding cassette) transporter MsbA in native-like lipid bilayer, which revealed the long-sought-after structural basis of MsbA-LPS interaction. We are actively pursuing the structures of MsbA in more conformational states in its functional cycle, all of which can serve as targets for drug development. We are now looking for collaborators interested in identification of potential novel targets for antibiotic development and structure guided in silico and chemical drug screening.