EXPANDING STRUCTURAL BIOLOGY AT WEST COAST
The Biomolecular cryoEM Facility at University California - Santa Cruz is a leading provider of cutting-edge structural biology solutions using transmission electron microscopy.
CryoEM at UCSC provides access to a complete workflow from sample analysis and optimization to grid preparation, automated high-resolution imaging, data analysis, tridimensional reconstruction, which allows structure determination via model construction and validation.
Multiple levels of service and access are available and correspond with the type of analysis desired. Onsite individual training is provided for users from different levels and there are no geographical restrictions.
Why not join our community? Get in touch today to learn more.
Meet the Team
Our lab works to identify the structural and biochemical underpinnings of biological timekeeping by circadian clocks, which synchronize physiology and behavior with the day/night cycle. By developing a mechanistic understanding of how molecular circadian clocks function, we aim to capitalize on the temporal regulation of physiology and behavior to develop innovative strategies to treat a broad spectrum of human diseases. Cryo-EM is playing an increasingly large role in our work, as we seek to describe day/night changes in clock protein dynamics and the formation of large clock protein assemblies.
The Rubin laboratory is using cryo-electron microscopy to study mechanisms controlling cell division and why those mechanisms fail in cancer cells. They aim to determine atomic resolution structures of transcription factors that control gene expression during the cell division cycle and the enzymes that regulate those transcription factors. These molecular pictures are motivating new therapeutic strategies to target tumor cell proliferation. The Rubin lab uses the UCSC cryo-EM facility as an indispensable resource for sample preparation screening and data collection.
For more information visit: https://rubinlab.sites.ucsc.edu.
The Raskatov lab investigates the impact of amino acid sidechain modification on amyloid beta fibril formation. We are particularly interested in amino acid deamidation, oxidation and epimerization (racemization).