[gabia]

The vast majority of structures in the protein data bank are determined by crystallography, which involves putting the protein in a chemical cocktail that causes it to crystallize. The cocktail is very different to the chemical environment in which the protein functions, so an open question is whether the protein structure determined by crystallography (and hence learned by AlphaFold) is representative of the structure in it's natural environment.

It would be very interesting if there was a way to use computational techniques to go beyond what crystallography and other experimental techniques (Cryo) can accomplish and determine the protein structure in it's true biological setting. Some research into experimental methods for this include high power X-ray pulses.

Nonetheless, impressive work!