Structural Biology


David Eisenberg, Ph.D.

Principal Investigator

Paul Boyer Professor, HHMI, Molecular Biology Institute

University of California, Los Angeles

David Eisenberg is a Professor of Chemistry and Biochemistry and of Biological Chemistry at the University of California, Los Angeles, and Director of the UCLA-DOE Institute for Genomics and Proteomics. He received his undergraduate degree in biochemical sciences from Harvard College and his D.Phil. degree in theoretical chemistry from Oxford University. His postdoctoral research was on ice and water with Walter Kauzmann at Princeton and in protein crystallography with Richard Dickerson. Dr. Eisenberg is a member of the National Academy of Sciences and the Institute of Medicine. He is a recipient of the 2004 UCLA Seaborg Medal, the 2005 Harvard Westheimer Medal, and the 2008 Emily Gray Award from the Biophysical Society. He as an h-index of 148 with over 100,000 citations and is a world authority on the subject of structural biology.

Todd Yeates, Ph.D.

Professor, Department of Chemistry and Biochemistry

University of California, Los Angeles

In the area of protein crystallography, we are pursuing problems of both theoretical and practical interest. This includes the introduction of new equations for analyzing X-ray diffraction data for various forms of disorder. Our theoretical work has also addressed, and largely answered, the long-standing puzzle of why proteins crystallize preferentially in only a few strongly favored space group symmetries, out of 65 possibilities. That analysis led to the prediction that proteins would crystallize with much greater ease if they could be prepared synthetically in racemic form (i.e. as a mixture of the biological enantiomer and its mirror image synthesized from D-amino acids). We continue to promote this as a future avenue for overcoming the problem of crystallizing macromolecules. In a separate line of attack, we have developed other strategies for crystallization based on a combination of protein engineering and chemical or metal-based ‘synthetic symmetrization’.


Jose Rodriguez, Ph.D.

Associate Professor, Department of Biochemistry

University of California, Los Angeles


Prof. Rodriguez studies the complex architecture of biological systems - from single biomolecules to cellular assemblies - at high resolution. His work is largely based on diffraction phenomena and combines computational, biochemical and biophysical experiments. The development of new methods is central to this work, particularly using emerging technologies in cryo-electron microscopy, nano and coherent x-ray diffraction, and macromolecular design. Combined, these tools can reveal undiscovered structures that broadly influence chemistry, biology, and medicine.

Larissa Podust, Ph.D.

Associate Professor

Skaggs School of Pharmacy & Pharmaceutical Sciences

University of California, San Diego

My research is focused on the structure-aided drug discovery for diseases representing global health problems. I am principal investigator of an NIH R01 grant which has as its aim to discover and develop new therapy for Chagas Disease based on inhibition of parasite sterol biosynthesis. In collaboration with William Roush, Director of Medicinal Chemistry at Scripps Florida, and members of the Center for Discovery and Innovation in Parasitic Diseases, we have identified several promising chemical scaffolds including compounds that not only inhibit CYP51, a central enzyme in sterol biosynthesis, but which also inhibit parasite replication in a mouse model of infection. These the compounds are currently being "rationally" optimized through a productive collaboration using our structural biology advances, the medicinal chemistry expertise of Drs. Roush and Choi, and computational resources and structure-based drug-discovery expertise provided by Ruben Abagyan laboratory, UC San Diego Skaggs School of Pharmacy.

Larissa Podust.png