Melanie Ohi

I am fascinated by how proteins and nucleic acids organize into dynamic structures. Although our categorization of the number and assortment of protein interactions is increasing, we still lack knowledge about how collections of proteins are precisely assembled into macromolecular machines.  My research program is positioned to attack this formidable challenge. 

Generating three-dimensional (3D) snapshots of protein complexes and molecular machines is invaluable for generating comprehensive mechanistic models.  Yet, the dynamic nature of many protein assemblies makes them inherently difficult to study using traditional structural approaches, such as X-ray crystallography. A promising, and rapidly advancing technique for obtaining macromolecular structural information is cryo-electron microscopy (cryo-EM). By combining molecular EM with complementary structural, biochemical, biophysical and genetic methods, as well as, embracing a collaborative multi-team approach, we aim to address the molecular basis underling important biological processes even when no atomic resolution structures are available. Our research goal is to generate detailed molecular models that will provide biological insight into function. 


  • Research Associate Professor, U-M Life Sciences Institute
  • Associate Professor, Cell and Developmental Biology, Medical School


  • B.S., Chemistry, Pacific Lutheran University, Tacoma, Wash.
  • Ph.D., Cell Biology, Vanderbilt University, laboratory of Dr. Kathy Gould
  • Jane Coffin Childs Postdoctoral Fellow, Harvard Medical School, laboratory of Tom Walz 

Honors & Awards

  • NIH New Innovator Award, 2008