Evidence map›Paper›PMID 25075337›Full record

ArticleIUCrJ2014

Avoidable errors in deposited macromolecular structures: an impediment to efficient data mining.

Zbigniew Dauter, Alexander Wlodawer, Wladek Minor, Mariusz Jaskolski, Bernhard Rupp

Abstract read
In one paragraph

Article in IUCrJ, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing 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

43 citing papers in PubMed.

  1. Avoiding pitfalls when modelling ligands in macromolecular crystallography.Acta crystallographica. Section D, Structural biology · 2026
    Article
  2. Scotty: lattice coincidences in the Protein Data Bank.Acta crystallographica. Section D, Structural biology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Duplicate entries in the Protein Data Bank: how to detect and handle them.Acta crystallographica. Section D, Structural biology · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Vagabond: bond-based parametrization reduces overfitting for refinement of proteins.Acta crystallographica. Section D, Structural biology · 2021
    Article
  14. CERES: a cryo-EM re-refinement system for continuous improvement of deposited models.Acta crystallographica. Section D, Structural biology · 2021
    Article
  15. Article
  16. Article
  17. Nucleobase carbonyl groups are poor MgRNA (New York, N.Y.) · 2019
    Article
  18. Article
  19. Review
  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

5 authors.

Zbigniew DauterSynchrotron Radiation Research Section, Macromolecular Crystallography Laboratory, NCI , Argonne National Laboratory, Argonne, IL 60439, USA.
Alexander WlodawerProtein Structure Section, Macromolecular Crystallography Laboratory, NCI at Frederick , Frederick, MD 21702, USA.
Wladek MinorDepartment of Molecular Physiology and Biological Physics, University of Virginia , Charlottesville, VA 22908, USA ; Midwest Center for Structural Genomics , USA ; New York Structural Genomics Consortium , USA ; Center for Structural Genomics of Infectious Diseases , USA ; Enzyme Function Initiative, USA.
Mariusz JaskolskiDepartment of Crystallography, Faculty of Chemistry, A. Mickiewicz University , Poznan, Poland ; Center for Biocrystallographic Research, Institute of Bioorganic Chemistry, Polish Academy of Sciences , Poznan, Poland.
Bernhard Ruppk.-k. Hofkristallamt , 991 Audrey Place, Vista, CA 92084, USA ; Department of Genetic Epidemiology, Innsbruck Medical University , Schöpfstrasse 41, A-6020 Innsbruck, Austria.

Funding

Core H: MicrobiologyU54GM093342 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI GERLT, JOHN A · 2010 to 2015
$34.6M
Midwest Center for Structural GenomicsU54GM094585 · NIGMS · UNIVERSITY OF CHICAGO · PI MINOR, WLADEK · 2010 to 2014
$33.7M
The NYSGRC: A Large Scale Center for PSI:BiologyU54GM094662 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI FISER, ANDRAS · 2010 to 2014
$32.6M
Protein StructureZIABC010348 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI WLODAWER, ALEXANDER · 2009 to 2025
$27.5M
X-RAY CRYSTALLOGRAPHY OF MACROMOLECULESR01GM053163 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI MINOR, WLADEK, OTWINOWSKI, ZBYSZEK · 1996 to 2014
$6.3M
NIAID NIH HHS HHSN272201200026CNIGMS NIH HHS R01 GM053163NIGMS NIH HHS U54 GM093342NIGMS NIH HHS U54 GM094585NIGMS NIH HHS U54 GM094662
6 · The paper itself

Abstract

Whereas the vast majority of the more than 85 000 crystal structures of macromolecules currently deposited in the Protein Data Bank are of high quality, some suffer from a variety of imperfections. Although this fact has been pointed out in the past, it is still worth periodic updates so that the metadata obtained by global analysis of the available crystal structures, as well as the utilization of the individual structures for tasks such as drug design, should be based on only the most reliable data. Here, selected abnormal deposited structures have been analysed based on the Bayesian reasoning that the correctness of a model must be judged against both the primary evidence as well as prior knowledge. These structures, as well as information gained from the corresponding publications (if available), have emphasized some of the most prevalent types of common problems. The errors are often perfect illustrations of the nature of human cognition, which is frequently influenced by preconceptions that may lead to fanciful results in the absence of proper validation. Common errors can be traced to negligence and a lack of rigorous verification of the models against electron density, creation of non-parsimonious models, generation of improbable numbers, application of incorrect symmetry, illogical presentation of the results, or violation of the rules of chemistry and physics. Paying more attention to such problems, not only in the final validation stages but during the structure-determination process as well, is necessary not only in order to maintain the highest possible quality of the structural repositories and databases but most of all to provide a solid basis for subsequent studies, including large-scale data-mining projects. For many scientists PDB deposition is a rather infrequent event, so the need for proper training and supervision is emphasized, as well as the need for constant alertness of reason and critical judgment as absolutely necessary safeguarding measures against such problems. Ways of identifying more problematic structures are suggested so that their users may be properly alerted to their possible shortcomings.

Indexed as

macromolecular crystallographymodel validationProtein Data Bank

Identifiers

PMID25075337
PMCPMC4086436

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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.