Evidence map›Paper›PMID 19564689›Full record

ArticleActa crystallographica. Section D, Biological crystallography2009

Interpretation of very low resolution X-ray electron-density maps using core objects.

Philipp Heuser, Gerrit G Langer, Victor S Lamzin

Abstract read
In one paragraph

Article in Acta crystallographica. Section D, Biological crystallography, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Automated identification of crystallographic ligands using sparse-density representations.Acta crystallographica. Section D, Biological crystallography · 2014
    Article
  2. 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

3 authors.

Philipp HeuserHamburg Unit, European Molecular Biology Laboratory, c/o DESY, Notkestrasse 85, Hamburg 22603, Germany. philipp.heuser@embl-hamburg.de
Gerrit G Langer
Victor S Lamzin

Funding

Unified automated model building & refinement for biological crystallographyR01GM062612 · NIGMS · EUROPEAN MOLECULAR BIOLOGY LABORATORY · PI LAMZIN, VICTOR S. · 2002 to 2009
$1.5M
NIGMS NIH HHS R01 GM062612NIGMS NIH HHS R01 GM62612
6 · The paper itself

Abstract

A novel approach to obtaining structural information from macromolecular X-ray data extending to resolutions as low as 20 A is presented. Following a simple map-segmentation procedure, the approximate shapes of the domains forming the structure are identified. A pattern-recognition comparative analysis of these shapes and those derived from the structures of domains from the PDB results in candidate structural models that can be used for a fit into the density map. It is shown that the placed candidate models can be employed for subsequent phase extension to higher resolution.

Indexed as

BacteriaBacterial ProteinsCrystallography, X-RayDatabases, ProteinElectronsModels, MolecularMutagensProtein MultimerizationProtein Structure, QuaternaryProtein Structure, TertiaryBacterial ProteinsMutagens

Identifiers

PMID19564689
PMCPMC2703575

What OpenQuestion holds

Textmetadata
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.