Journal
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
Volume 78, Issue -, Pages 1-13Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2059798321012122
Keywords
protein structure prediction; crystallographic phase problem; molecular replacement; AlphaFold2
Funding
- Wellcome Trust Principal Research Fellowship [209407/Z/17/Z]
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The results of AlphaFold2 in CASP14 indicate that accurate predictions of protein structure domains are on the horizon, regardless of their similarity to known structures. As highly accurate models are generated using correlated mutations and deep learning, methods of phasing in crystallography, especially molecular-replacement phasing using in silico models, are expected to be impacted.
The AlphaFold2 results in the 14th edition of Critical Assessment of Structure Prediction (CASP14) showed that accurate (low root-mean-square deviation) in silico models of protein structure domains are on the horizon, whether or not the protein is related to known structures through high-coverage sequence similarity. As highly accurate models become available, generated by harnessing the power of correlated mutations and deep learning, one of the aspects of structural biology to be impacted will be methods of phasing in crystallography. Here, the data from CASP14 are used to explore the prospects for changes in phasing methods, and in particular to explore the prospects for molecular-replacement phasing using in silico models.
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