CryoEM reveals the structure of a two-component archaeal S-layer, which sheds new light on archaeal cell biology.

The surface layer of Sulfolobus acidocaldarius consists of a flexible but stable outer protein layer that interacts with an inner, membrane-bound protein.

The crenarchaeon Sulfolobus synthesizes the N-glycan core in the identical way as all Eukaryotes, which strengthens the hypothesis that the eukaryotic N-glycosylation is acquired from an ancient archaeon during eukaryogenesis.

Using both electron cryo-tomography and helical reconstruction, the first structure of the entire archaellum machinery with an assembled filament has been determined, providing the structural basis for our understanding of archaeal motility.

An archaeal basal transcription factor containing an iron-sulphur cluster sheds light on the evolution of transcription machineries in archaea and eukaryotes.

Synechocystis switches its redox pools under reducing photomixotrophic conditions from utilizing NAD(H)- to ferredoxin-dependent enzymes and thereby balances its metabolism in a trade-off between energy conservation and chemical driving forces.

The archaeal MCM helicase can load in multiple orientations on DNA but translocation proceeds with a leading N-terminal domain, which affects double hexamer activation at origins of replication.

By using mass spectrometry, we determined the global levels of various DNA modifications across species and tissues.

Structures of binary and ternary complexes of DinG reveal translocation mechanism of XPD family helicases.

An investigation into 8-oxodeoxguanosine bypass by archaeal DNA polymerases.