The integration of cryo-EM data into our data-driven docking program HADDOCK and its performance on a benchmark of 17 complexes is described in a recently published Structure article. The approach is demonstrated on five systems using experimental cryo-EM data in the range of 8.5–21 Å resolution. For several cases, cryo-EM data are integrated with additional interface information, e.g. mutagenesis and hydroxyl radical footprinting data. The resulting models have high-quality interfaces, revealing novel details of the interactions.
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Computational Structural Biology group focusing on dissecting, understanding and predicting biomolecular interactions at the molecular level.
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