Exploring de novo Phasing with Protein Models
Author Information
Author(s): Das Rhiju, Baker David
Primary Institution: University of Washington
Hypothesis
Can de novo models effectively phase diffraction data for proteins with new folds?
Conclusion
De novo models can phase diffraction data for approximately one sixth of proteins with sizes of 100 residues or less, but require significant computational resources.
Supporting Evidence
- All-atom refinement significantly improves model quality.
- 15 new cases of diffraction data sets were successfully phased.
- Larger proteins required less accurate models for successful phasing.
Takeaway
This study shows that we can use new computer models to help figure out the structure of proteins we've never seen before, but it takes a lot of computer power to do it.
Methodology
The study involved systematic exploration of phasing with Rosetta de novo models, testing all-atom refinement and computational power on 30 diffraction data sets.
Limitations
The method requires significant computational resources, which may limit its practical application.
Statistical Information
P-Value
p<0.05
Statistical Significance
p<0.05
Digital Object Identifier (DOI)
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