Evidence map›Paper›PMID 29652255›Full record

ArticleActa crystallographica. Section D, Structural biology2018

Gyre and gimble: a maximum-likelihood replacement for Patterson correlation refinement.

Airlie J McCoy, Robert D Oeffner, Claudia Millán, Massimo Sammito, Isabel Usón, Randy J Read

Abstract read
In one paragraph

Article 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 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. ARCIMBOLDO at low resolution: Verification for coiled coils and globular proteins.Protein science : a publication of the Protein Society · 2024
    Article
  2. Verification: model-free phasing with enhanced predicted models in ARCIMBOLDO_SHREDDER.Acta crystallographica. Section D, Structural biology · 2022
    Article
  3. Article
  4. ALIXE: a phase-combination tool for fragment-based molecular replacement.Acta crystallographica. Section D, Structural biology · 2020
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Identification of the active site residues in ATP-citrate lyase's carboxy-terminal portion.Protein science : a publication of the Protein Society · 2019
    Article
  10. Ega3 from the fungal pathogenThe Journal of biological chemistry · 2019
    Article
  11. Article
  12. Article
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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

6 authors.

Airlie J McCoyDepartment of Haematology, Cambridge Institute for Medical Research, University of Cambridge, Hills Road, Cambridge CB2 0XY, England.
Robert D OeffnerDepartment of Haematology, Cambridge Institute for Medical Research, University of Cambridge, Hills Road, Cambridge CB2 0XY, England.ORCID 0000-0003-3107-2202
Claudia MillánCrystallographic Methods, Institute of Molecular Biology of Barcelona (IBMB-CSIC), Barcelona Science Park, Helix Building, Baldiri Reixac 15, 08028 Barcelona, Spain.ORCID 0000-0002-9283-2220
Massimo SammitoCrystallographic Methods, Institute of Molecular Biology of Barcelona (IBMB-CSIC), Barcelona Science Park, Helix Building, Baldiri Reixac 15, 08028 Barcelona, Spain.ORCID 0000-0002-8346-9247
Isabel UsónCrystallographic Methods, Institute of Molecular Biology of Barcelona (IBMB-CSIC), Barcelona Science Park, Helix Building, Baldiri Reixac 15, 08028 Barcelona, Spain.
Randy J ReadDepartment of Haematology, Cambridge Institute for Medical Research, University of Cambridge, Hills Road, Cambridge CB2 0XY, England.ORCID 0000-0001-8273-0047

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
Biotechnology and Biological Sciences Research Council BB/L006014/1NIGMS NIH HHS P01 GM063210Wellcome Trust 082961/Z/07/ZWellcome Trust 209407/Z/17/Z
6 · The paper itself

Abstract

Descriptions are given of the maximum-likelihood gyre method implemented in Phaser for optimizing the orientation and relative position of rigid-body fragments of a model after the orientation of the model has been identified, but before the model has been positioned in the unit cell, and also the related gimble method for the refinement of rigid-body fragments of the model after positioning. Gyre refinement helps to lower the root-mean-square atomic displacements between model and target molecular-replacement solutions for the test case of antibody Fab(26-10) and improves structure solution with ARCIMBOLDO_SHREDDER.

Indexed as

Likelihood FunctionsModels, MolecularCrystallography, X-RayDatabases, ProteinHumansImmunoglobulin Fab FragmentsProtein ConformationRotationSoftwareImmunoglobulin Fab Fragmentsantibodiescrystallographic phasingfragment-based molecular replacementmaximum likelihoodPatterson correlation refinement

Identifiers

PMID29652255
PMCPMC5892877

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.