A fully automated benchmarking suite to compare macromolecular complexes

Protein structure prediction has a long history of benchmarking efforts such as critical assessment of structure prediction, continuous automated model evaluation and critical assessment of prediction of interactions. With the rise of artificial intelligence-based methods for prediction of macromolecular complexes, benchmarking with large datasets and robust, unsupervised scores to compare predictions against a reference has become essential. Also, the increasing size and complexity of experimentally determined reference structures by crystallography or cryogenic electron microscopy poses challenges for structure comparison methods. Here we review the current state of the art in scoring methodologies, identify existing limitations and present more suitable approaches for scoring of tertiary and quaternary structures, protein-protein interfaces and protein-ligand complexes. Our methods are designed to scale efficiently, enabling the assessment of large, complex systems. All developments are available in the structure benchmarking framework of OpenStructure. OpenStructure is open source software and available for free at https://openstructure.org/ .

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Publication Details

Journal
Nature Methods
Published
2025-12-22
DOI
https://doi.org/10.1038/s41592-025-02973-z
Citations
1
Primary Topic
Protein Structure and Dynamics
Type
article
Field-Weighted Citation Impact
0.81
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article

A fully automated benchmarking suite to compare macromolecular complexes

Xavier Robin, Stefan Bienert, Torsten Schwede, Peter Škrinjar et al.
1 citations
Nature Methods
Protein Structure and Dynamics
0.81
article

A fully automated benchmarking suite to compare macromolecular complexes

Xavier Robin, Stefan Bienert, Torsten Schwede, Peter Škrinjar, Andrew Mark Waterhouse, Gerardo Tauriello, Janani Durairaj, Gabriel Studer
article en
1 citations

Abstract

Protein structure prediction has a long history of benchmarking efforts such as critical assessment of structure prediction, continuous automated model evaluation and critical assessment of prediction of interactions. With the rise of artificial intelligence-based methods for prediction of macromolecular complexes, benchmarking with large datasets and robust, unsupervised scores to compare predictions against a reference has become essential. Also, the increasing size and complexity of experimentally determined reference structures by crystallography or cryogenic electron microscopy poses challenges for structure comparison methods. Here we review the current state of the art in scoring methodologies, identify existing limitations and present more suitable approaches for scoring of tertiary and quaternary structures, protein-protein interfaces and protein-ligand complexes. Our methods are designed to scale efficiently, enabling the assessment of large, complex systems. All developments are available in the structure benchmarking framework of OpenStructure. OpenStructure is open source software and available for free at https://openstructure.org/ .

Nature MethodsVol. 23(2)
SIB Swiss Institute of Bioinformatics (CH), University of Basel (CH)
Openalex Percentile: Top 20%
Protein Structure and Dynamics
0.81
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A fully automated benchmarking suite to compare macromolecular complexes — Xavier Robin, Stefan Bienert, et al. · Nature Methods (2025) | TGRS Research Map | TGRS