Jason T. Kaelber

The paper reports structures of long-range coupled transcription-translation complexes (TTC-LC) in E. coli, showing how they differ from TTC-B and their roles in transcription-translation coupling.

This study determines the cryo-EM structure of the AAV2 Rep-capsid packaging complex, revealing how Rep proteins interact with the capsid and contribute to genome packaging.

This study presents cryo-EM structures of ArnC, revealing its conformational changes and catalytic mechanism for aminoarabinose glycosylation in polymyxin resistance.

The paper demonstrates using optical interference in a cryogenic FIB-SEM-LM system to target lamella production beyond the diffraction limit for capturing virions in host cells.

The paper reports the structure of the archaeal FttA pre-termination complex using cryo-EM, revealing its mechanism of action and functional homology with bacterial and eukaryotic systems.

Cryo-EM reveals the structural basis of transcription-translation coupling by RfaH.

The paper reports cryo-EM structures of functional Rho pre-termination complexes in Escherichia coli, explaining their mechanism and resolving decades of research.

This paper reports atomic structures of Qλ, showing it forms a nozzle to prevent RNA hairpin formation, unlike Q21, and uses a different mechanism and loading process involving NusA.

This study investigates reiterative transcription initiation, showing RNA extension occurs without DNA scrunching, involves a short RNA-DNA hybrid, and uses an alternative RNA exit pathway.

The paper uses cryo-EM to define structural states of transcription-translation complexes in bacteria that mediate NusG- and NusA-dependent coupling.

The paper reports high-resolution structures of Q protein states during antitermination, showing Q forms a nozzle that narrows the RNA-exit channel and prevents RNA hairpin formation.