Evidence map›Paper›PMID 28232893›Full record

ArticleIntrinsically disordered proteins2015

Missing strings of residues in protein crystal structures.

Kristina Djinovic-Carugo, Oliviero Carugo

Abstract read
In one paragraph

Article in Intrinsically disordered proteins, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. MultilevelCurrent research in structural biology · 2026
    Article
  2. Article
  3. Crystal structure of the folded domains of Xrs2 from Saccharomyces cerevisiae.Acta crystallographica. Section F, Structural biology communications · 2025
    Article
  4. AFFIPred: AlphaFold2 structure-based Functional Impact Prediction of missense variations.Protein science : a publication of the Protein Society · 2025
    Article
  5. Article
  6. Anti-angiogenic Potential of Trans-chalcone in anCardiovascular & hematological agents in medicinal chemistry · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Current approaches to flexible loop modeling.Current research in structural biology · 2021
    Review
  15. Simple Selection Procedure to Distinguish between Static and Flexible Loops.International journal of molecular sciences · 2020
    Article
  16. Review
  17. Article
  18. Article
  19. 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

2 authors.

Kristina Djinovic-CarugoDepartment of Structural and Computational Biology; Max F. Perutz Laboratories, Vienna University, Vienna Biocenter (VBC); Vienna, Austria; Department of Biochemistry; Faculty of Chemistry and Chemical Technology, University of Ljubljana; Ljubljana, Slovenia.
Oliviero CarugoDepartment of Structural and Computational Biology; Max F. Perutz Laboratories, Vienna University, Vienna Biocenter (VBC); Vienna, Austria; Department of Chemistry; Pavia University; Pavia, Italy.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A large fraction of the protein crystal structures deposited in the Protein Data Bank are incomplete, since the position of one or more residues is not reported, despite these residues are part of the material that was analyzed. This may bias the use of the protein crystal structures by molecular biologists. Here we observe that in the large majority of the protein crystal structures strings of residues are missing. Polar residues incline to occur in missing strings together with glycine, while apolar and aromatic residues tend to avoid them. Particularly flexible residues, as shown by their extremely high B-factors, by their exposure to the solvent and by their secondary structures, flank the missing strings. These data should be a helpful guideline for crystallographers that encounter regions of flat and uninterpretable electron density as well as end-users of crystal structures.

Indexed as

conformational disorderdisordered proteinsmissing atomsmissing residuesprotein crystal structureprotein data bankstructural bioinformaticsunfolded proteins

Identifiers

PMID28232893
PMCPMC5314880

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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.