SAXS of huntingtin – a different approach to assess the structure of this protein

We have generated some really interesting data from our cryo-EM studies of the huntingtin protein to date. Susan Lea and Justin Deme who are working on the HTT samples I send from Toronto, recently shared this screen capture of the huntingtin envelopes from the most recent sample which are super to see:

Huntingtin Q23 cryo-EM envelope – calculated by Professor Susan Lea and Dr Justin Deme

As a complementary and orthogonal approach to understanding the huntingtin protein structure, I am keen to try small-angle X-ray scattering (SAXS). Although low resolution, this approach will allow calculation of the protein envelope in solution which will be interesting to compare to that calculated by cryo-EM where the sample is vitrified in a layer of thin ice.

To do these experiments, I need to make more huntingtin protein. You can see my sample preparation on Zenodo. The SAXS experiments are being completed by these folks soon – here’s hoping for some interesting data.

3 thoughts on “SAXS of huntingtin – a different approach to assess the structure of this protein

  1. LabScribbles/R.Harding: Reading what I read, you are preparing huntingtin protein samples from bacteria, so HTT is a bacteria-based linked protein. So why not compare a bacteria-based linked protein like HTT to an antibacterial-based linked protein? Here’s one to consider: Platypus Milk’s “Shirlrey Temple” @ https://www.gizmodo.com.au/2018/03/platypus-milk-shirley-temple-protein-could-be-key-to-its-powerful-antibacterial-properties/ I’m going off here in a tangent again, nevertheless, it is an interesting article to read. Enjoy :-).

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