There are many reasons for anti-intellectualism, but in the current moment, much of it is political. We’re in a rightwing, segregationist backlash & colleges are viewed as bastions of progressiveness and integration AND sources of an alternative form of authority, making them dangerous to fascists.

Yes indeed.

That’s what seems to be happening, yes.

Most if not all study sections this week didn’t happen. Panels can be found via the following link. Asterisk denotes that the meeting didn’t take place as scheduled.

www.csr.nih.gov/RevPanelsAnd...

Congratulations to all authors for their contributions, and especially to lead author Khuram Ashraf. A big thank you to @pstansfeld.bsky.social and Jason Kaelber for collaborating with us. We acknowledge NIH for funding support, and we also thank NCCAT staff for help with the Krios collection. 9/n

Finally, we propose a catalytic scheme that employs two separate coordination positions for the acceptor phosphate within the catalytic domain, and a reaction mechanism that likely operates in all similar enzymes of the polyprenyl phosphate glycosyltransferase family. 8/n

And, with the help of Mariana Bunoro-Batista and @pstansfeld.bsky.social we perform detailed atomistic simulations with both donor and acceptor substrates to fully describe substrate binding and identify catalytic residues in this enzyme. 7/n

With the help of Bertie Ansell and @pstansfeld.bsky.social, we perform coarse-grained simulations to show that the acceptor lipid UndP threads between the juxtamembrane helices of an ArnC protomer to reach the catalytic GT-A domain. 6/n

WIth the help of Jason Kaelber, we perform a comparison of the two apo ArnC datasets collected on a 200kV Talos Arctica and a 300kV Titan Krios microscope using duplicate grids, to examine whether a higher quality microscope/detector can meaningfully improve the reconstruction for this sample. 5/n

We describe a conformational transition that occurs upon binding of the partial substrate UDP, moving the catalytic GT-A domain closer to the membrane. 4/n

For the UDP-bound state, we observed clear non-protein density within the binding cavity of the catalytic GT-A domain, which we modeled as UDP coordinated by a Mn2+ metal ion. 3/n