Evangel Nogales De La Morena
Biophysicist Senior Faculty Scientist
Building: Stanley Hall, Room 708C
Mail Stop: STANLEY
Phone: (510) 642-0557
Fax: (510) 666-3336
ENogales@lbl.gov
Links
Research Interests
cryo-EM, biochemistry, complex biological assemblies, structure and regulation of the cytoskeleton, microtubule dynamics, human transcriptional initiation machinery, epigenetics, gene silencing, biophysics
Eva Nogales is a senior faculty scientist, Professor of Biochemistry, Biophysics and Structural Biology, and a Howard Hughes Investigator. The Nogales Lab is dedicated to gaining mechanistic insight into crucial molecular processes in the life of the eukaryotic cell. Their two main research themes are the dynamic self-assembly of cytoskeleton during its essential functions in cell division, and the molecular machines governing the regulation of gene expression, specially at the transcriptional level. The unifying principle in their work is the emphasis on studying macromolecular assemblies as whole units of molecular function by direct visualization of their architecture, functional states and regulatory interactions. With this overall aim in mind they use electron microscopy and image analysis, complemented with biochemical and biophysical assays, towards a molecular understanding of their systems of interest.
Recent Publications
Related News
Nogales Garners Two International Accolades
In December, Eva Nogales, senior faculty scientist Molecular Biophysics and Integrated Bioimaging (MBIB) Division, traveled to her native Spain where she was honored for her work in the field of visualization of macromolecular function.
Nogales Named 2023 Shaw Prize Laureate
Biophysicist Eva Nogales, a senior faculty scientist in the Molecular Biophysics and Integrated Bioimaging Division, is a 2023 recipient of the Shaw Prize in Life Science and Medicine. Nogales shares the prize with Patrick Cramer of the Max Planck Institute for Multidisciplinary Sciences in Germany.
Cryo-EM Reveals Blueprint for Microbial Photosynthesis
Advances in cryogenic electron microscopy have enabled an international team of experts to visualize the structure of a cyanobacterial phycobilisome with nearly atomic resolution. The work, a collaboration among researchers at Michigan State University, UC Berkeley, Berkeley Lab, and the University of South Bohemia in the Czech Republic, was published in Nature. Knowing the position of different proteins and pigments helps scientist better understand this natural process and can inspire future applications in areas such as renewable energy and environmental remediation.
