Congrats Martin!

Congrats Martin and best of luck!

Congrats Sveta and the team!!

Congratulations!

Looks familiar - also from a FLAG IP in HEK cells.

Very nice work, congratulations Sam and the team!

Our data suggest that mitochondrial ribosome biogenesis and translation initiation are not strictly sequential, but can occur simulatenously with MTG3 acting as a quality control factor.

This is really mindblowing stuff, congrats again Florent, Ben and the team!

Please see the paper for more details! Please also see the great complementary work by Rachel Fearns & Jonathan Abrahams: www.cell.com/cell/fulltex...
and the several other complementary papers published recently describing the apo structure of the NiV polymerase complex.

Comparisons between the two structures show how rearrangements of key elements in the RdRp upon RNA binding lead to large-scale reorganisation of the complex and ordering of the C-terminal domains required for RNA capping.

The structure reveals how NiV RdRp interacts with template and product RNA and with the incoming substrate nucleoside triphosphate during RNA synthesis. To our knowledge, this represents the first structure of a non-segmented negative-strand RNA virus RdRp in this state.

By using a non-hydrolyzable GTP-analog, we were additionally able to visualise the RdRp after de novo synthesis of 9 nt of product RNA. In this early replicating state, the C-terminal domains of L become stabilised and visible in the cryo-EM reconstruction.

The NiV RNA-dependent RNAP (RdRp) adopts an architecture similar to that of other negative strand RNA viruses such as Ebola or RSV, in which four copies of P protein protrude from the core formed by L. In the apo state, the C-terminal domains of L are mobile and hence invisible.