Abstract
CASP (Critical Assessment of Structure prediction) conducts community
experiments to determine the state of the art in computing protein
structure from amino acid sequence. The process relies on the
experimental community providing information about not yet public or
about to be solved structures, for use as targets. For some targets, the
experimental structure is not solved in time for use in CASP. Calculated
structure accuracy improved dramatically in this round, implying that
models should now be much more useful for resolving many sorts of
experimental difficulty. To test this, selected models for seven
unsolved targets were provided to the experimental groups. These models
were from the AlphaFold2 group, who overall submitted the most accurate
predictions in CASP14. Four targets were solved with the aid of the
models, and, additionally, the structure of an already solved target was
improved. An a-posteriori analysis showed that in some cases models from
other groups would also be effective. This paper provides accounts of
the successful application of models to structure determination,
including molecular replacement for X-ray crystallography, backbone
tracing and sequence positioning in a Cryo-EM structure, and correction
of local features. The results suggest that in future there will be
greatly increased synergy between computational and experimental
approaches to structure determination.