Evidence map›Paper›PMID 27980519›Full record

ArticleJournal of applied crystallography2016

Arnaud Hungler, Afaque Momin, Kay Diederichs, Stefan T Arold

Abstract read
In one paragraph

Article in Journal of applied crystallography, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Scotty: lattice coincidences for macromolecular crystallographic phasing.Acta crystallographica. Section D, Structural biology · 2026
    Article
  2. Cryo-EM reveals ArnA contamination during purification of a ciliary protein complex.Acta crystallographica. Section D, Structural biology · 2026
    Article
  3. The Starting Point for Biomolecular Crystallisation.Advances in biochemical engineering/biotechnology · 2026
    Review
  4. Article
  5. Serendipitous high-resolution structure of Escherichia coli carbonic anhydrase 2.Acta crystallographica. Section F, Structural biology communications · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Crystal structure of the Escherichia coli transcription termination factor Rho.Acta crystallographica. Section F, Structural biology communications · 2020
    Article
  12. Contamination or serendipity - doing the wrong thing by chance.Acta crystallographica. Section F, Structural biology communications · 2020
    Article
  13. Detecting the nature and solving the crystal structure of a contaminant protein from an opportunistic pathogen.Acta crystallographica. Section F, Structural biology communications · 2020
    Article
  14. Article
  15. Article
  16. Article
  17. Making routine native SAD a reality: lessons from beamline X06DA at the Swiss Light Source.Acta crystallographica. Section D, Structural biology · 2019
    Article
  18. Article
  19. SIMBAD: a sequence-independent molecular-replacement pipeline.Acta crystallographica. Section D, Structural biology · 2018
    Article
  20. 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

4 authors.

Arnaud HunglerKing Abdullah University of Science and Technology (KAUST) , Center for Computational Bioscience Research (CBRC), Division of Biological and Environmental Sciences and Engineering (BESE), Thuwal, 23955-6900, Saudi Arabia.
Afaque MominKing Abdullah University of Science and Technology (KAUST) , Center for Computational Bioscience Research (CBRC), Division of Biological and Environmental Sciences and Engineering (BESE), Thuwal, 23955-6900, Saudi Arabia.
Kay DiederichsFachbereich Biologie, Universität Konstanz , M647, D-78457 Konstanz, Germany.
Stefan T AroldKing Abdullah University of Science and Technology (KAUST) , Center for Computational Bioscience Research (CBRC), Division of Biological and Environmental Sciences and Engineering (BESE), Thuwal, 23955-6900, Saudi Arabia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Solving the phase problem in protein X-ray crystallography relies heavily on the identity of the crystallized protein, especially when molecular replacement (MR) methods are used. Yet, it is not uncommon that a contaminant crystallizes instead of the protein of interest. Such contaminants may be proteins from the expression host organism, protein fusion tags or proteins added during the purification steps. Many contaminants co-purify easily, crystallize and give good diffraction data. Identification of contaminant crystals may take time, since the presence of the contaminant is unexpected and its identity unknown. A webserver (

Indexed as

computer programscontaminant crystalsdiffractionmolecular replacement

Identifiers

PMID27980519
PMCPMC5140001

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.