Cryo-EM targets in CASP14

By Tristan Cragnolini, Andriy Kryshtafovych, Maya Topf. 2021

10 citations recorded by the source corpus.

Structures of seven CASP14 targets were determined using cryo‐electron microscopy (cryo‐EM) technique with resolution between 2.1 and 3.8 Å. We provide an evaluation of the submitted models versus the experimental data (cryo‐EM density maps) and experimental reference structures built into the maps. The accuracy of models is measured in terms of coordinate‐to‐density and coordinate‐to‐coordinate fit. A‐posteriori refinement of the most accurate models in their corresponding cryo‐EM density resulted in structures that are close to the reference structure, including some regions with better fit to the density. Regions that were found to be less “refineable” correlate well with regions of high diversity between the CASP models and low goodness‐of‐fit to density in the reference structure.

Subfields: Materials Chemistry, Molecular Biology, Radiation

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Materials Chemistry

In Molecular Biology

Citations in the corpus

Assessment of three-dimensional RNA structure prediction in CASP15 (2023, neutral): “Indeed, for all four non-natural RNA targets in CASP15 (Table 1), the AIchemy_RNA2 group (TS232) submitted models that were visually accurate (Figure 1).”
CASP15 cryoEM protein and RNA targets: refinement and analysis using experimental maps (2023, methodology): “As per the CASP13 and CASP14 modeling experiments 1,2 , predictions of cryoEM targets were positioned in the density by aligning them to the target and then optimizing local fit to density before refinement using ChimeraX fit-to-map function.”