Welcome to the

Kollman Lab

Welcome to the

Kollman Lab

Structural studies of intracellular organization

We are examining the structures of the complex macromolecular machinery of cellular organization, with a focus on bacterial cytoskeletal systems and organelles.  Our structural approach centers on cryo-electron microscopy, which we combine with X-ray crystallography.  This integrative approach allows us to generate mechanistic insights over a broad range of size and resolution scales.

recent publications

We trapped a closed conformation of the yeast γTuRC, demonstrating that it can function as a perfect microtubule template.  The structure of the closed state allowed us to make an atomic model of a capped microtubule minus end.

Kollman JM, Greenberg CH, Li S, Moritz M, Zelter A, Fong KFF, Fernandez J-J, Sali A, Kilmartin J, Davis TN, Agard DA.  (2015) Ring closure activates yeast γTuRC for species-specific microtubule nucleation. Nat. Struct. Mol. Biol.  [PMID 25030911][pdf]

CTP synthetase assembles filamentous polymers, which we and our collaborators show are enzymatically inactive.  This represents a novel mechanism of enzyme regulation.  Our cryo-EM structre, at 8.4 Å resolution provides insight into the mechanisms of filament assembly and enzyme inhibition.

Barry RM, Bitbol AF, Lorestani A, Charles EJ, Habrian CH, Hansen JM, Li HJ, Baldwin EP, Wingreen NS, Kollman JM, Gitai Z (2014) Large-scale filament formation inhibits the activity of CTP synthase. eLife 2014;10.7554 [PMID 25030911][pdf]

In the free form the adaptor protein AlfB disrupts AlfA filament assembly and bundling, but the AlfB-DNA complex promotes filament assembly and tracks the end of growing filaments

Polka JK, Kollman JM, Mullins RD (2014)  Accessory factors promote AlfA-dependent plasmid segregation by regulating filament nucleation, disassembly, and bundling [PMID24481252] [pdf]

1959 NE Pacific Street Box 357350

Seattle, WA 98195