Evidence map›Paper›PMID 40401365›Full record

ArticleProteins2025

Using AlphaFold and Symmetrical Docking to Predict Protein-Protein Interactions for Exploring Potential Crystallization Conditions.

Kuan-Ju Liao, Yuh-Ju Sun

Abstract read
In one paragraph

Article in Proteins, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Article
  2. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Kuan-Ju LiaoInstitute of Bioinformatics and Structural Biology, National Tsing Hua University, Taiwan.
Yuh-Ju SunInstitute of Bioinformatics and Structural Biology, National Tsing Hua University, Taiwan.ORCID 0000-0003-4734-7848

Funding

National Science and Technology CouncilNational Tsing Hua University
6 · The paper itself

Abstract

Protein crystallization remains a major bottleneck in X-ray crystallography due to difficulties in achieving favorable molecular arrangements within the crystal lattice. While protein-protein interactions at molecular packing interfaces are crucial for determining crystallization conditions, methods for predicting crystal packing interfaces and systematically exploring crystallization conditions remain limited. In this study, we present MASCL (Molecular Assembly Simulation in Crystal Lattice), a novel approach that integrates AlphaFold with symmetrical docking to simulate crystal packing. To evaluate packing quality, we introduced PackQ, a stringent metric based on the DockQ framework, where models with scores above 0.36 are considered successful. In benchmark tests on P4

Indexed as

Molecular Docking SimulationMuramidaseProtein Interaction MappingProteinsSoftwareAlgorithmsCrystallizationCrystallography, X-RayProtein BindingProtein ConformationMuramidaseProteinsAlphaFoldcrystallization condition explorationcrystal packing interfacemolecular surfaceprotein–protein interactionX‐ray crystallography

Identifiers

PMID40401365
PMCPMC12433261

What OpenQuestion holds

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LicenceCC BY-NC
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.