The Agard lab in the Department of Biochemistry & Biophysics at UCSF has multiple postdoc openings. Their group is focused on understanding the molecular basis by which the Hsp70 and Hsp90 molecular chaperones regulate cytosolic protein folding and function as couple to downstream processes such as nuclear entry and lysosomal degradation via chaperone-mediated autophagy. Both single particle and cryoET projects are available. UCSF provides a remarkably rich environment for pursuing state-of-the-art cryoEM as well as broader structural and cellular biology research in a vibrant and dynamic city.
The candidate should have a PhD or equivalent in structural biology, biophysics, or cell biology and a deep interest in molecular mechanisms. While helpful, no prior experience in electron cryo-EM or cryoET is required. Candidates should contact Dr. Agard agard@msg.ucsf.edu and include a CV, indication of research interests, and contact information for three references.
Examples of their recent molecular chaperone published efforts (Nature 2022):
Structure of Hsp90-Hsp70-Hop-GR reveals the Hsp90 client-loading mechanism.
Wang RY, Noddings CM, Kirschke E, Myasnikov AG, Johnson JL, Agard DA
Structure of Hsp90-p23-GR reveals the Hsp90 client-remodelling mechanism.
Noddings CM, Wang RY, Johnson JL, Agard DA
Also very recent cryoET
Electron cryo-tomography structure of axonemal doublet microtubule from Tetrahymena thermophila.
Li S, Fernandez JJ, Fabritius AS, Agard DA, Winey M
Zheng S, Wolff G, Greenan G, Chen Z, Faas FGA, Bárcena M, Koster AJ, Cheng Y, Agard DA
