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 dynamic interplay between type III CRISPR enzymes governs cyclic nucleotide levels and infection outcomes in virus-host conflict.

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.

Generation of the anti-viral second messenger cyclic oligoadenylate by type III CRISPR systems is tightly controlled in response to viral RNA load and sequence.

Building on previous work (Froelich et al., 2014), we present the X-ray crystal structure of an active MCM hexamer, which suggests a mechanism for MCM regulation and demonstrates a key interaction between the major domains.

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.

The acquisition of new foreign DNA by the prokaryotic adaptive immune system CRISPR-Cas is shown to depend on the fundamental sequence specificity of the Cas1 integrase.

The Mcm2-7 motor unwinds DNA using an approach distinct from that of superfamily III helicases, and accesses multiple ring configurations and assembly states during the initiation of DNA replication.

Archaeal histones compact DNA into nucleosome-like particles of varying sizes that contort sporadically and reorient DNA wrapping.