Quality assessment for molecular models: Difference between revisions

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 There are several free automated servers that can improve most published models. See [[Improving published models]].
-Recently, new methods for protein structure validation  based on the compatibility of a structure with the inter-residue distances and contacts predicted by methods such as AlphaFold 2 have been introduced <ref]https://pubmed.ncbi.nlm.nih.gov/36458613/</ref>. Then all 3-5Å resolution cryo-EM and crystallogrpahic structures in the PDB with that method, identifying thousands of likely register errors via these scans for locally incorrect PDB structures <ref>https://www.biorxiv.org/content/10.1101/2024.07.19.604304</ref>.
+Recently, new methods for protein structure validation based on the compatibility of a structure with the inter-residue distances and contacts predicted by methods such as AlphaFold 2 have been introduced <ref>PMID: 36458613/</ref>. Then all 3-5Å resolution cryo-EM and crystallographic structures in the PDB with that method, identifying thousands of likely register errors via these scans for locally incorrect PDB structures <ref>https://www.biorxiv.org/content/10.1101/2024.07.19.604304</ref>.
 ==Further Reading==