Evidence map›Paper›PMID 30847635›Full record

ArticleJournal of biomolecular NMR2019

Accuracy and precision of protein structures determined by magic angle spinning NMR spectroscopy: for some 'with a little help from a friend'.

Ryan W Russell, Matthew P Fritz, Jodi Kraus, Caitlin M Quinn, Tatyana Polenova, Angela M Gronenborn

Open access · greenAbstract read
In one paragraph

Article in Journal of biomolecular NMR, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

19 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. bioRxiv : the preprint server for biology · 2026
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  4. bioRxiv : the preprint server for biology · 2025
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  7. IntegratingJournal of the American Chemical Society · 2024
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  18. Integrative methods in structural biology.Journal of biomolecular NMR · 2019
    Article
  19. 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

6 authors at 1 institution in 1 country.

Ryan W RussellDepartment of Chemistry and Biochemistry, University of Delaware, 19716, Newark, DE, USA.
Matthew P FritzDepartment of Chemistry and Biochemistry, University of Delaware, 19716, Newark, DE, USA.
Jodi KrausDepartment of Chemistry and Biochemistry, University of Delaware, 19716, Newark, DE, USA.
Caitlin M QuinnDepartment of Chemistry and Biochemistry, University of Delaware, 19716, Newark, DE, USA.
Tatyana PolenovaDepartment of Chemistry and Biochemistry, University of Delaware, 19716, Newark, DE, USA. tpolenov@udel.edu.ORCID http://orcid.org/0000-0002-0346-1131
Angela M GronenbornPittsburgh Center for HIV Protein Interactions, University of Pittsburgh School of Medicine, 1051 Biomedical Science Tower 3, 3501 Fifth Ave, 15261, Pittsburgh, PA, USA. amg100@pitt.edu.
University of Pittsburgh · US

Funding

X-Ray Core P50GM082251 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI ENGELMAN, ALAN N. · 2007 to 2018
$48.1M
Technology Development 2: MAS NMR and dynamic nuclear polarization for HIV-1 structural biologyP50AI150481 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI GRONENBORN, ANGELA M. · 2019 to 2021
$14.1M
Pilot Research Subproject ProgramP30GM110758 · NIGMS · UNIVERSITY OF DELAWARE · PI PATEL, SANDEEP · 2014 to 2018
$5.8M
NIAID NIH HHS P50 AI150481NIGMS NIH HHS P30 GM110758NIGMS NIH HHS P30GM110758NIGMS NIH HHS P50 GM082251NIGMS NIH HHS P50GM082251
6 · The paper itself

Abstract

We present a systematic investigation into the attainable accuracy and precision of protein structures determined by heteronuclear magic angle spinning solid-state NMR for a set of four proteins of varied size and secondary structure content. Structures were calculated using synthetically generated random sets of C-C distances up to 7 Å at different degrees of completeness. For single-domain proteins, 9-15 restraints per residue are sufficient to derive an accurate model structure, while maximum accuracy and precision are reached with over 15 restraints per residue. For multi-domain proteins and protein assemblies, additional information on domain orientations, quaternary structure and/or protein shape is needed. As demonstrated for the HIV-1 capsid protein assembly, this can be accomplished by integrating MAS NMR with cryoEM data. In all cases, inclusion of TALOS-derived backbone torsion angles improves the accuracy for small number of restraints, while no further increases are noted for restraint completeness above 40%. In contrast, inclusion of TALOS-derived torsion angle restraints consistently increases the precision of the structural ensemble at all degrees of distance restraint completeness.

Indexed as

Models, MolecularNuclear Magnetic Resonance, BiomolecularProtein ConformationAmino Acid SequenceCapsid ProteinsCryoelectron MicroscopyProteinsReproducibility of ResultsCapsid ProteinsProteinsIntegrated structural biologyMagic angle spinningProtein structure calculation

Identifiers

PMID30847635
PMCPMC6693955
OpenAlexW2921643031

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

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.