Evidence map›Paper›PMID 30082516›Full record

ReviewActa crystallographica. Section D, Structural biology2018

Evaluation of models determined by neutron diffraction and proposed improvements to their validation and deposition.

Dorothee Liebschner, Pavel V Afonine, Nigel W Moriarty, Paul Langan, Paul D Adams

Open access · hybridAbstract readReview
In one paragraph

Review in Acta crystallographica. Section D, Structural biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

11 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Improved joint X-ray and neutron refinement procedure in Phenix.Acta crystallographica. Section D, Structural biology · 2023
    Article
  3. Neutron crystallographic refinement with REFMAC5 from the CCP4 suite.Acta crystallographica. Section D, Structural biology · 2023
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. 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

5 authors at 3 institutions in 2 countries.

Dorothee LiebschnerMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
Pavel V AfonineMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.ORCID 0000-0002-5052-991X
Nigel W MoriartyMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.ORCID 0000-0001-8857-9464
Paul LanganNeutron Science Directorate, Oak Ridge National Laboratory, PO Box 2008, Oak Ridge, TN 37831, USA.
Paul D AdamsMolecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
Lawrence Berkeley National Laboratory · USOak Ridge National Laboratory · USShanghai University · CN

Funding

PROJECT 5 - DUKE - STRUCTURE VALIDATION AND IMPROVEMENT FOR PROTEINS AND N. ACIDSP01GM063210 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI ADAMS, PAUL DAVID · 2001 to 2021
$33.5M
Computational Tools for Neutron Protein CrystallographyR01GM071939 · NIGMS · UT-BATTELLE, LLC-OAK RIDGE NATIONAL LAB · PI COATES, LEIGHTON · 2004 to 2019
$4.3M
NIGMS NIH HHS P01 GM063210NIGMS NIH HHS R01 GM071939
6 · The paper itself

Abstract

The Protein Data Bank (PDB) contains a growing number of models that have been determined using neutron diffraction or a hybrid method that combines X-ray and neutron diffraction. The advantage of neutron diffraction experiments is that the positions of all atoms can be determined, including H atoms, which are hardly detectable by X-ray diffraction. This allows the determination of protonation states and the assignment of H atoms to water molecules. Because neutrons are scattered differently by hydrogen and its isotope deuterium, neutron diffraction in combination with H/D exchange can provide information on accessibility, dynamics and chemical lability. In this study, the deposited data, models and model-to-data fit for all PDB entries that used neutron diffraction as the source of experimental data have been analysed. In many cases, the reported R

Indexed as

Models, MolecularDatabases, ProteinDeuterium Exchange MeasurementMacromolecular SubstancesNeutron DiffractionProteinsMacromolecular SubstancesProteinsH/D exchangemodel validationneutron crystallographyPDB data miningPhenix

Identifiers

PMID30082516
PMCPMC6079631
OpenAlexW2882999099

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.