Evidence map›Paper›PMID 33404521›Full record

ArticleActa crystallographica. Section D, Structural biology2021

Using a partial atomic model from medium-resolution cryo-EM to solve a large crystal structure.

Montserrat Fàbrega-Ferrer, Ana Cuervo, Francisco J Fernández, Cristina Machón, Rosa Pérez-Luque, Joan Pous, M Cristina Vega, José L Carrascosa, Miquel Coll

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 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Review
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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

9 authors.

Montserrat Fàbrega-FerrerInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Baldiri Reixac 10, 08028 Barcelona, Spain.ORCID 0000-0001-9471-0473
Ana CuervoCentro Nacional de Biotecnología (CNB-CSIC), Darwin 3, 28049 Madrid, Spain.
Francisco J FernándezCentro de Investigaciones Biológicas (CIB-CSIC), Ramiro de Maeztu 9, 28040 Madrid, Spain.
Cristina MachónInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Baldiri Reixac 10, 08028 Barcelona, Spain.
Rosa Pérez-LuqueInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Baldiri Reixac 10, 08028 Barcelona, Spain.
Joan PousInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Baldiri Reixac 10, 08028 Barcelona, Spain.
M Cristina VegaCentro de Investigaciones Biológicas (CIB-CSIC), Ramiro de Maeztu 9, 28040 Madrid, Spain.
José L CarrascosaCentro Nacional de Biotecnología (CNB-CSIC), Darwin 3, 28049 Madrid, Spain.
Miquel CollInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Baldiri Reixac 10, 08028 Barcelona, Spain.

Funding

Ministerio de Ciencia, Innovación y Universidades BFU2014-53550-PMinisterio de Ciencia, Innovación y Universidades BFU2014-54181Ministerio de Ciencia, Innovación y Universidades BFU2017-83720-PMinisterio de Ciencia, Innovación y Universidades MDM-2014-0435Ministerio de Ciencia, Innovación y Universidades RYC-2011-09071Ministerio de Ciencia, Innovación y Universidades SEV-2013-0347Ministerio de Ciencia, Innovación y Universidades SEV-2015-0500
6 · The paper itself

Abstract

Medium-resolution cryo-electron microscopy maps, in particular when they include a significant number of α-helices, may allow the building of partial models that are useful for molecular-replacement searches in large crystallographic structures when the structures of homologs are not available and experimental phasing has failed. Here, as an example, the solution of the structure of a bacteriophage portal using a partial 30% model built into a 7.8 Å resolution cryo-EM map is shown. Inspection of the self-rotation function allowed the correct oligomerization state to be determined, and density-modification procedures using rotation matrices and a mask based on the cryo-EM structure were critical for solving the structure. A workflow is described that may be applicable to similar cases and this strategy is compared with direct use of the cryo-EM map for molecular replacement.

Indexed as

Bacteriophage T7Capsid ProteinsCryoelectron MicroscopyModels, MolecularProtein ConformationSoftwareCapsid Proteinsbacteriophage portalcryo-EMdensity modificationmolecular replacement

Identifiers

PMID33404521
PMCPMC7787105

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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.