The lab's first paper is published in Science!

Exciting genomic engineering possibilities exist for natural integration systems, called transposons, which have co-opted CRISPR/Cas systems. How insertions occur in a single orientation at a precise distance from the protospacer has been enigmatic. It has been mysterious how the transposase (TnsB) is recruited by the ATPase TnsC to the point of insertion marked by TniQ. We find orientation of the integration event is set by polar growth of a TnsC filament terminated at TniQ. TnsB dissociates TnsC filaments in a process driving the search for new TniQ-programed integration sites. Fixed TnsC structures found as hydrolysis intermediates suggest a spacing mechanism marking the precise point of TnsB-mediated insertion.  This model suggests multiple avenues for engineering these systems.

https://science.sciencemag.org/content/early/2021/07/14/science.abi8976

Eshan is killing it!

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The Department of Chemistry and Chemical Biology has selected Eshan Mehrotra as the recipient of the 2021 Leo and Berdie Mandelkern Prize, in recognition of his academic excellence in chemistry.

In addition, Eshan is featured in the Cornell Chronicle (in the lab, his native environment!) We are so proud of you, Eshan!

https://physics.cornell.edu/news/i-gained-deep-appreciation-interplay-between-theory-and-experiment-physics

Our first paper is published!

In collaboration with Don Rio’s lab at UC Berkeley, we report a 3.6 Å resolution cryo-EM structure of the P element transposase strand-transfer (i.e. transpososome) complex. Not only did we encounter severe preferential orientation issues (which we overcame with tilting), we had to build the entire structure (nearly 900 amino acids) de novo!

https://www.nature.com/articles/s41594-019-0319-6


See the accompanying (and excellent!) news&views written by Phoebe Rice.

https://www.nature.com/articles/s41594-019-0329-4

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