Evidence map›Paper›PMID 34449113›Full record

ArticleProteins2021

Computational models in the service of X-ray and cryo-electron microscopy structure determination.

Andriy Kryshtafovych, John Moult, Reinhard Albrecht, Geoffrey A Chang, Kinlin Chao, Alec Fraser, Julia Greenfield, Marcus D Hartmann, Osnat Herzberg, Inokentijs Josts and 9 more

Open access · greenAbstract read
In one paragraph

Article in Proteins, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.3field-weighted citation impact, top 7% of its field
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

30 citing papers in PubMed, 48 citations in OpenAlex.

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  16. Structural and enzymatic characterization of the sialidase SiaPG from Porphyromonas gingivalis.Acta crystallographica. Section F, Structural biology communications · 2023
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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

19 authors at 7 institutions in 3 countries.

Andriy KryshtafovychGenome Center, University of California, Davis, California, USA.ORCID 0000-0002-8185-1215
John MoultInstitute for Bioscience and Biotechnology Research, Department of Cell Biology and Molecular genetics, University of Maryland, Rockville, Maryland, USA.
Reinhard AlbrechtDepartment of Protein Evolution, Max Planck Institute for Developmental Biology, Tübingen, Germany.
Geoffrey A ChangSkaggs School of Pharmacy and Pharmaceutical Sciences, University of California-San Diego, La Jolla, California, USA.
Kinlin ChaoInstitute for Bioscience and Biotechnology Research, University of Maryland, Rockville, Maryland, USA.
Alec FraserDepartment of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics (SCSB), The University of Texas Medical Branch at Galveston, Galveston, Texas, USA.
Julia GreenfieldInstitute for Bioscience and Biotechnology Research, University of Maryland, Rockville, Maryland, USA.
Marcus D HartmannDepartment of Protein Evolution, Max Planck Institute for Developmental Biology, Tübingen, Germany.ORCID 0000-0001-6937-5677
Osnat HerzbergInstitute for Bioscience and Biotechnology Research, University of Maryland, Rockville, Maryland, USA.
Inokentijs JostsThe Hamburg Advanced Research Center for Bioorganic Chemistry (HARBOR) & Department of Chemistry, Institute for Biochemistry and Molecular Biology, University of Hamburg, Hamburg, Germany.
Petr G LeimanDepartment of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics (SCSB), The University of Texas Medical Branch at Galveston, Galveston, Texas, USA.
Sara B LindenInstitute for Bioscience and Biotechnology Research, University of Maryland, Rockville, Maryland, USA.
Andrei N LupasDepartment of Protein Evolution, Max Planck Institute for Developmental Biology, Tübingen, Germany.
Daniel C NelsonInstitute for Bioscience and Biotechnology Research, University of Maryland, Rockville, Maryland, USA.
Steven D ReesSkaggs School of Pharmacy and Pharmaceutical Sciences, University of California-San Diego, La Jolla, California, USA.
Xiaoran ShangInstitute for Bioscience and Biotechnology Research, University of Maryland, Rockville, Maryland, USA.
Maria L SokolovaCenter of Life Sciences, Skolkovo Institute of Science and Technology, Moscow, Russia.
Henning TidowThe Hamburg Advanced Research Center for Bioorganic Chemistry (HARBOR) & Department of Chemistry, Institute for Biochemistry and Molecular Biology, University of Hamburg, Hamburg, Germany.
AlphaFold2 teamDeepMind, London, UK.
University of Maryland, Baltimore · USMax Planck Institute for Developmental Biology · DEThe University of Texas Medical Branch at Galveston · USUniversität Hamburg · DEUniversity of California San Diego · USSkolkovo Institute of Science and Technology · RUUniversity of California, Davis · US

Funding

Prospective analysis to determine model accuracy performance and boundaries in the post-AlphaFold2 environmentR01GM100482 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI FIDELIS, KRZYSZTOF A · 2012 to 2025
$11.1M
Structural and functional determinants of decision-making in bacteriophage host recognitionR01GM139034 · NIGMS · UNIVERSITY OF TEXAS MED BR GALVESTON · PI LEIMAN, PETR G · 2020 to 2023
$1.7M
Structure, Function, and Engineering of Myovirus Phage CBA120 Tailspike ProteinsR01GM110202 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI NELSON, DANIEL C. · 2015 to 2019
$1.5M
Medical Research Council G0600084Medical Research Council MR/N009614/1NIGMS NIH HHS R01 GM100482NIGMS NIH HHS R01 GM110202NIGMS NIH HHS R01 GM139034
6 · The paper itself

Abstract

Critical assessment of structure prediction (CASP) conducts community experiments to determine the state of the art in computing protein structure from amino acid sequence. The process relies on the experimental community providing information about not yet public or about to be solved structures, for use as targets. For some targets, the experimental structure is not solved in time for use in CASP. Calculated structure accuracy improved dramatically in this round, implying that models should now be much more useful for resolving many sorts of experimental difficulties. To test this, selected models for seven unsolved targets were provided to the experimental groups. These models were from the AlphaFold2 group, who overall submitted the most accurate predictions in CASP14. Four targets were solved with the aid of the models, and, additionally, the structure of an already solved target was improved. An a posteriori analysis showed that, in some cases, models from other groups would also be effective. This paper provides accounts of the successful application of models to structure determination, including molecular replacement for X-ray crystallography, backbone tracing and sequence positioning in a cryo-electron microscopy structure, and correction of local features. The results suggest that, in future, there will be greatly increased synergy between computational and experimental approaches to structure determination.

Indexed as

Cryoelectron MicroscopyCrystallography, X-RayModels, MolecularComputational BiologyProtein ConformationProteinsSoftwareProteinsCASPcryo-EMprotein structure predictionX-ray crystallography

Identifiers

PMID34449113
PMCPMC8616789
OpenAlexW3194187547

What OpenQuestion holds

Textmetadata
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Registered trials

None linked

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.