Was an honor to help our collaborator Judith Klinman celebrate her 80th birthday last weekend in Berkeley, with @klinmanlab members, colleagues, friends, and family!! Lots of great science highlights, and some sage advice too...

This is a long overdue tweet, but earlier this month we FINALLY (after 2 years) moved from our dusty, old "temporary" lab space, to our fancy, fresh, and brand new lab!! 🤩 Feels good to have a permanent home on campus, just in time for the Fall semester...

Back to work after a great week at the @ProteinSociety Annual Symposium!! #PS36 This conference always has such cool science, and is always a great chance to see old friends and make new ones. Obligatory lab photo:

Special shout out to @irisdyoung, who, in addition to being a data/programming guru, also speaks Japanese and is something of a ramen afficionado!! A big help in navigating the Shinkansen, and mealtimes. (29/32)

Alex also came along from @ucsf to @ucmerced to help start a lab and see this project through to the end. I appreciate his bravery!! Here we are celebrating the @biorxiv submission. (27/32)

This project was a big collaboration, and there are lots of people to thank! Some of them are pictured here at SACLA. (23/32)

Inhibitor binding, which is known to slow active site opening/closing, seems to prevent the dissipation of fast motions into larger amplitude (functional) conformational changes observed in the apo enzyme. (21/32)

Time-resolved changed to the electron density are much more pronounced for the apo enzyme than for the inhibitor-bound enzyme. (20/32)

Are the motions we observed related to function? One of the major loop rearrangements we see (res 97-100) involves a helix that bends when the lysozyme active site closes. We also looked at lysozyme bound to an inhibitor (chitobiose). (19/32)

At longer pump-probe time delays (200 microseconds), we see evidence that the “heating effects” observed at 20 ns have dissipated into larger motions, including rearrangements of the backbone. (18/32)