Vadim Molodtsov

This paper characterizes OLD, an abortive immunity protein, revealing its structure and activation mechanism in response to phage replication and DNA defects in RecBCD-compromised cells.

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.

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 transcription-translation complexes (TTCs) at different stages of the translation cycle in E. coli, revealing structural changes and their functional implications.

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

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

This study reports the X-ray crystal structures of E. coli RNA polymerase complexes with DksA and ppGpp, revealing how ppGpp enhances DksA's inhibition of transcription initiation.