My group is interested in understanding how large macromolecular machines couple energy, in the form of nucleotide hydrolysis, to conformational changes and in the functional roles played by these structural rearrangements. We have focused on chromatin dynamics and intracellular transport. We use a combination of cell biological, biochemical, biophysical and structural approaches with a particular focus on cryo-electron microscopy (cryo-EM).
Research Focus Areas
Biochemistry and Structural Biology | Gene Expression and Regulation
Cianfrocco M and Leschziner AE (2015) Low cost, high performance processing of single particle cryo-electron microscopy data in the cloud. eLife: 06664
Toropova K*, Zou S*, Roberts AJ, Redwine WB, Goodman BS, Reck-Peterson SL# and Leschziner AE# (2014). Lis1 regulates dynein by sterically blocking its mechanochemical cycle. eLife 3:e03372. PMC4359366.
Nguyen VQ, Ranjan A, Stengel F, Wei D, Aebersold R, Wu C and Leschziner AE (2013). Molecular architecture of the ATP-dependent chromatin remodeling complex SWR1. Cell 154(6): 1220-31. PMC3776929.
Redwine WB*, Hernandez-Lopez R*, Zou S, Huang J, Reck-Peterson SL and Leschziner AE (2012). Structural basis for microtubule binding and release by dynein. Science 337(6101): 1532-6. PMC3919166.
Huang J*, Roberts AJ*, Leschziner AE and Reck-Peterson SL (2012). Lis1 acts as a “clutch” between the ATPase and microtubule-binding domains of the dynein motor. Cell 150: 1-12. PMC3438448.
Chandramouli P, Hernandez-Lopez R, Wang, HW and Leschziner AE (2011). Validation of the orthogonal tilt reconstruction method with a biological test sample. J Struct Biol. 175:85-96.
* co-first authorship
# co-corresponding authorship