Elizabeth Villa Rodriguez | |
|---|---|
| Alma mater | University of Illinois Urbana-Champaign National Autonomous University of Mexico |
| Scientific career | |
| Institutions | Max Planck Institute of Biochemistry University of California, San Diego |
| Thesis | Multiscale Modeling of Biomolecular Complexes (2008) |
Elizabeth Villa is an American biophysicist who is Associate Professor at theUniversity of California, San Diego. Her research considers the development ofCryo Electron Tomography and structural biology. She was named aHoward Hughes Medical Institute Research Investigator in 2021.
Villa grew up inMexico, which is where she first studied physics.[1] She earned her doctorate at theUniversity of Illinois Urbana-Champaign, where she worked as a Fulbright Fellow. She completed her research in the laboratory ofKlaus Schulten on the modeling of biomolecular complexes.[2] During her doctorate, she was introduced tocryogenic electron microscopy, and worked withJoachim Frank on approaches to combineX-ray crystallography withCryo EM andmolecular dynamics.[3] She moved to theMax Planck Institute of Biochemistry as aMarie Skłodowska-Curie Actions as a postdoctoral fellow.[4]
Villa joined the Department of Chemistry at theUniversity of California, San Diego in 2014. She was selected aPew Research Scholar in 2017.[5] In 2021, Villa was named aHoward Hughes Medical Institute Fellow.[6]
Villa has developed novel techniques to explore cellular machinery.[7] This machinery includes bulky molecular complexes, which are composed of nucleic acids, carbohydrates and proteins. Her early work developed tags forCryo Electron Tomography (cryo-ET), for which she was awarded anNational Institutes of Health Director's Award.[8][9][10] She developed cryofocused ion beam milling, which makes use of an ion beam to remove ultra-thin layers of cellular material. Images can be acquired from various angles using atransmission electron microscope and reconstructed to form a three-dimensional picture.[11]
Villa determined the structure of theLRRK2 protein. Mutations in LRRK2 are the most frequent cause ofParkinson's disease.[12][13] The protein includes a 14 Å structure with apathogenic mutation that forms a right-handed double helix around left-handed tubules.[12] By understanding the 3D structure of LRRK2, Villa hopes to design new treatments for Parkinson's disease.[14]
{{cite journal}}:Cite journal requires|journal= (help)