ArticleActa crystallographica. Section D, Structural biology2018
Ensembles generated from crystal structures of single distant homologues solve challenging molecular-replacement cases in AMPLE.
Article in Acta crystallographica. Section D, Structural biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed.
- The success rate of processed predicted models in molecular replacement: implications for experimental phasing in the AlphaFold era.Acta crystallographica. Section D, Structural biology · 2024Article
- Modes and model building in SHELXE.Acta crystallographica. Section D, Structural biology · 2024Article
- Predicted models and CCP4.Acta crystallographica. Section D, Structural biology · 2023Article
- The Automatic Solution of Macromolecular Crystal Structures via Molecular Replacement Techniques: REMO22 and Its Pipeline.International journal of molecular sciences · 2023Article
- MrParse: finding homologues in the PDB and the EBI AlphaFold database for molecular replacement and more.Acta crystallographica. Section D, Structural biology · 2022Article
- Implications of AlphaFold2 for crystallographic phasing by molecular replacement.Acta crystallographica. Section D, Structural biology · 2022Review
- Redeployment of automated MrBUMP search-model identification for map fitting in cryo-EM.Acta crystallographica. Section D, Structural biology · 2021Article
- Introduction to molecular replacement: a time perspective.Acta crystallographica. Section D, Structural biology · 2021Review
- Helical ensembles outperform ideal helices in molecular replacement.Acta crystallographica. Section D, Structural biology · 2020Article
- Fragment-based determination of a proteinase K structure from MicroED data using ARCIMBOLDO_SHREDDER.Acta crystallographica. Section D, Structural biology · 2020Article
- SEQUENCE SLIDER: expanding polyalanine fragments for phasing with multiple side-chain hypotheses.Acta crystallographica. Section D, Structural biology · 2020Article
- How far are we from automatic crystal structure solution via molecular-replacement techniques?Acta crystallographica. Section D, Structural biology · 2020Article
- Molecular replacement using structure predictions from databases.Acta crystallographica. Section D, Structural biology · 2019Article
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7 authors.
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Abstract
Molecular replacement (MR) is the predominant route to solution of the phase problem in macromolecular crystallography. Although routine in many cases, it becomes more effortful and often impossible when the available experimental structures typically used as search models are only distantly homologous to the target. Nevertheless, with current powerful MR software, relatively small core structures shared between the target and known structure, of 20-40% of the overall structure for example, can succeed as search models where they can be isolated. Manual sculpting of such small structural cores is rarely attempted and is dependent on the crystallographer's expertise and understanding of the protein family in question. Automated search-model editing has previously been performed on the basis of sequence alignment, in order to eliminate, for example, side chains or loops that are not present in the target, or on the basis of structural features (e.g. solvent accessibility) or crystallographic parameters (e.g. B factors). Here, based on recent work demonstrating a correlation between evolutionary conservation and protein rigidity/packing, novel automated ways to derive edited search models from a given distant homologue over a range of sizes are presented. A variety of structure-based metrics, many readily obtained from online webservers, can be fed to the MR pipeline AMPLE to produce search models that succeed with a set of test cases where expertly manually edited comparators, further processed in diverse ways with MrBUMP, fail. Further significant performance gains result when the structure-based distance geometry method CONCOORD is used to generate ensembles from the distant homologue. To our knowledge, this is the first such approach whereby a single structure is meaningfully transformed into an ensemble for the purposes of MR. Additional cases further demonstrate the advantages of the approach. CONCOORD is freely available and computationally inexpensive, so these novel methods offer readily available new routes to solve difficult MR cases.
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