In 2021, I was involved in a study of the #chromatin remodeler ALC1, a protein involved in the early events of the DNA damage response. This led to a paper summarized in a previous thread: https://fediscience.org/@Guillawme/111534984107819771

We had deposited the raw #cryoEM data to #EMPIAR (dataset EMPIAR-10739), which is the primary reason this new preprint could come to exist at all.

This figure shows the structural knowledge available on ALC1 up to the point of the new structure we report in the preprint. An AlphaFold2 prediction, a structure of the auto-inhibited conformation, and a few structures of ALC1-nucleosome complexes. Notably, none of the structures of nucleosome complexes resolved the macro domain. This is a significant gap, because the macro domain is key in regulating ALC1: it is responsible for auto-inhibition and recruitment to PARylated nucleosomes, and these two things are exclusive, which is why recruitment also causes release of the auto-inhibition. So at this point we know what the protein looks like when auto-inhibited and when active, but how it transitions from the former to the latter is unclear.

2/5

@jeremyforest @jonny

Hosting scientific data in the corporate cloud is a bad idea, given current costs and the volatility of the digital storage industry.

Projects like #EMPIAR https://www.ebi.ac.uk/empiar/ seems more capable and likely to survive into the future.