Jenkins, Huw Thomas orcid.org/0000-0002-3302-6966 (2018) Fragon: rapid high-resolution structure determination from ideal protein fragments. Acta crystallographica. Section D, Structural biology. pp. 205-214. ISSN 2059-7983
Abstract
Correctly positioning ideal protein fragments by molecular replacement presents an attractive method for obtaining preliminary phases when no template structure for molecular replacement is available. This has been exploited in several existing pipelines. This paper presents a new pipeline, named Fragon, in which fragments (ideal α-helices or β-strands) are placed using Phaser and the phases calculated from these coordinates are then improved by the density-modification methods provided by ACORN. The reliable scoring algorithm provided by ACORN identifies success. In these cases, the resulting phases are usually of sufficient quality to enable automated model building of the entire structure. Fragon was evaluated against two test sets comprising mixed α/β folds and all-β folds at resolutions between 1.0 and 1.7 Å. Success rates of 61% for the mixed α/β test set and 30% for the all-β test set were achieved. In almost 70% of successful runs, fragment placement and density modification took less than 30 min on relatively modest four-core desktop computers. In all successful runs the best set of phases enabled automated model building with ARP/wARP to complete the structure.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | Publisher Copyright: © 2018 Jenkins 2018. |
Keywords: | density modification,protein fragments,Fragon,molecular replacement,Algorithms,Proteins/analysis,Computer Simulation,Humans,Models, Molecular,Crystallography, X-Ray,Protein Conformation,Software |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Chemistry (York) |
Depositing User: | Pure (York) |
Date Deposited: | 09 Feb 2018 09:50 |
Last Modified: | 06 Jan 2025 00:11 |
Published Version: | https://doi.org/10.1107/S2059798318002292 |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1107/S2059798318002292 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:127271 |
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Filename: HJ_Fragon_ActaD_final.pdf
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Filename: Fragon_Acta_Cryst_D74_205_214.pdf
Description: Fragon_Acta_Cryst_D74_205-214
Licence: CC-BY 2.5
Filename: HJ_Fragon_ActaD_SI.pdf
Description: Supporting Information (Figures)
Filename: HJ_Fragon_ActaD_SI.xlsx
Description: Supporting Information (Details of test sets)