Evidence map›Paper›PMID 33559603›Full record

ArticleActa crystallographica. Section D, Structural biology2021

Detection of translational noncrystallographic symmetry in Patterson functions.

Iracema Caballero, Massimo D Sammito, Pavel V Afonine, Isabel Usón, Randy J Read, Airlie J McCoy

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 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. ARCIMBOLDO at low resolution: Verification for coiled coils and globular proteins.Protein science : a publication of the Protein Society · 2024
    Article
  3. Verification: model-free phasing with enhanced predicted models in ARCIMBOLDO_SHREDDER.Acta crystallographica. Section D, Structural biology · 2022
    Article
  4. Article
  5. Phasertng: directed acyclic graphs for crystallographic phasing.Acta crystallographica. Section D, Structural biology · 2021
    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.

Iracema CaballeroCrystallographic Methods, Institute of Molecular Biology of Barcelona (IBMB-CSIC), Baldiri Reixac 15, 08028 Barcelona, Spain.
Massimo D SammitoDepartment of Haematology, Cambridge Institute for Medical Research, University of Cambridge, Hills Road, Cambridge CB2 0XY, United Kingdom.
Pavel V AfonineLawrence Berkeley National Laboratory, One Cyclotron Road, BLDG 64R0121, Berkeley, CA 93720, USA.
Isabel UsónCrystallographic Methods, Institute of Molecular Biology of Barcelona (IBMB-CSIC), Baldiri Reixac 15, 08028 Barcelona, Spain.
Randy J ReadDepartment of Haematology, Cambridge Institute for Medical Research, University of Cambridge, Hills Road, Cambridge CB2 0XY, United Kingdom.ORCID 0000-0001-8273-0047
Airlie J McCoyDepartment of Haematology, Cambridge Institute for Medical Research, University of Cambridge, Hills Road, Cambridge CB2 0XY, United Kingdom.

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
NIGMS NIH HHS P01 GM063210NIH HHS P01GM063210Wellcome Trust 209407/Z/17/Z
6 · The paper itself

Abstract

Detection of translational noncrystallographic symmetry (TNCS) can be critical for success in crystallographic phasing, particularly when molecular-replacement models are poor or anomalous phasing information is weak. If the correct TNCS is detected then expected intensity factors for each reflection can be refined, so that the maximum-likelihood functions underlying molecular replacement and single-wavelength anomalous dispersion use appropriate structure-factor normalization and variance terms. Here, an analysis of a curated database of protein structures from the Protein Data Bank to investigate how TNCS manifests in the Patterson function is described. These studies informed an algorithm for the detection of TNCS, which includes a method for detecting the number of vectors involved in any commensurate modulation (the TNCS order). The algorithm generates a ranked list of possible TNCS associations in the asymmetric unit for exploration during structure solution.

Indexed as

Crystallography, X-RayAlgorithmsDatabases, ProteinLikelihood FunctionsModels, MolecularProtein ConformationProteinsProteinsintensity statisticsmaximum likelihoodmolecular replacementtranslational noncrystallographic symmetry

Identifiers

PMID33559603
PMCPMC7869901

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Registered trials

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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.