Evidence map›Paper›PMID 34726166›Full record

ArticleActa crystallographica. Section D, Structural biology2021

Redeployment of automated MrBUMP search-model identification for map fitting in cryo-EM.

Adam J Simpkin, Martyn D Winn, Daniel J Rigden, Ronan M Keegan

Abstract read
In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2021. 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

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3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Likelihood-based docking of models into cryo-EM maps.Acta crystallographica. Section D, Structural biology · 2023
    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

4 authors.

Adam J SimpkinInstitute of Structural, Molecular and Integrative Biology, University of Liverpool, Liverpool L69 7ZB, United Kingdom.
Martyn D WinnUKRI-STFC, Rutherford Appleton Laboratory, Research Complex at Harwell, Didcot OX11 0FA, United Kingdom.ORCID 0000-0003-0496-6796
Daniel J RigdenInstitute of Structural, Molecular and Integrative Biology, University of Liverpool, Liverpool L69 7ZB, United Kingdom.ORCID 0000-0002-7565-8937
Ronan M KeeganUKRI-STFC, Rutherford Appleton Laboratory, Research Complex at Harwell, Didcot OX11 0FA, United Kingdom.

Funding

Biotechnology and Biological Sciences Research Council BB/S007105/1Medical Research Council MR/N009614/1Medical Research Council MR/V000403/1
6 · The paper itself

Abstract

In crystallography, the phase problem can often be addressed by the careful preparation of molecular-replacement search models. This has led to the development of pipelines such as MrBUMP that can automatically identify homologous proteins from an input sequence and edit them to focus on the areas that are most conserved. Many of these approaches can be applied directly to cryo-EM to help discover, prepare and correctly place models (here called cryo-EM search models) into electrostatic potential maps. This can significantly reduce the amount of manual model building that is required for structure determination. Here, MrBUMP is repurposed to fit automatically obtained PDB-derived chains and domains into cryo-EM maps. MrBUMP was successfully able to identify and place cryo-EM search models across a range of resolutions. Methods such as map segmentation are also explored as potential routes to improved performance. Map segmentation was also found to improve the effectiveness of the pipeline for higher resolution (<8 Å) data sets.

Indexed as

SoftwareAnimalsCryoelectron MicroscopyDatabases, ProteinHumansModels, MolecularProtein ConformationProtein DomainsProteinsProteinscryo-EMGroELmolecular replacementMrBUMP

Identifiers

PMID34726166
PMCPMC8561737

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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.