Had a great time talking at @mgeworkshop.bsky.social last week and meeting some great people. Looking forward to cool science and collaborations to come.

Finally, we found that phiCD508 lacks identifiable enzymatic domains in the tail spike, suggesting the #phage breaks through by contractile force alone.

We also found that S-layer penetrating phages tend to have smaller tail spikes, lacking a beta-helical domain.

Surprisingly, we found that phiCD508 only contracts by about 20%, which is quite unusual. It also seems a reduced contraction is conserved amongst S-layer penetrating #phages

We were able to determine the structure of the #phage in both the extended and contracted states, and model the majority of the proteins making up the ~23MDa assembly

New paper alert 🚨

We determined the structure of phiCD508, a 225 nm tailed myovirus #phage infecting clinical strains of C. difficile, using #cryoEM.

Thrilled to see this finally out at @lsajournal.org .

www.life-science-alliance.org/content/8/6/...

Great to be back on Ava the Arctica at @molmicrosheffield.bsky.social, with a passable first grid prep also!