Evidence map›Paper›PMID 25372670›Full record

ArticleActa crystallographica. Section D, Biological crystallography2014

Covering complete proteomes with X-ray structures: a current snapshot.

Marcin J Mizianty, Xiao Fan, Jing Yan, Eric Chalmers, Christopher Woloschuk, Andrzej Joachimiak, Lukasz Kurgan

Open access · hybridAbstract read
In one paragraph

Article in Acta crystallographica. Section D, Biological crystallography, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.6field-weighted citation impact, top 17% of its field
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

12 citing papers in PubMed, 36 citations in OpenAlex.

  1. Accurate and Fast Prediction of Intrinsic Disorder Using flDPnn.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  2. PLMC: Language Model of Protein Sequences Enhances Protein Crystallization Prediction.Interdisciplinary sciences, computational life sciences · 2024
    Article
  3. Structural and functional analysis of "non-smelly" proteins.Cellular and molecular life sciences : CMLS · 2020
    Article
  4. Article
  5. Article
  6. Review
  7. ssbio: a Python framework for structural systems biology.Bioinformatics (Oxford, England) · 2018
    Article
  8. Article
  9. Article
  10. Article
  11. The impact of structural genomics: the first quindecennial.Journal of structural and functional genomics · 2016
    Review
  12. Structural genomics and the Protein Data Bank.The Journal of biological chemistry
    Review
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

7 authors at 2 institutions in 2 countries.

Marcin J MiziantyElectrical and Computer Engineering, University of Alberta, Edmonton, Alberta T6G 2V4, Canada.
Xiao FanElectrical and Computer Engineering, University of Alberta, Edmonton, Alberta T6G 2V4, Canada.
Jing YanElectrical and Computer Engineering, University of Alberta, Edmonton, Alberta T6G 2V4, Canada.
Eric ChalmersElectrical and Computer Engineering, University of Alberta, Edmonton, Alberta T6G 2V4, Canada.
Christopher WoloschukElectrical and Computer Engineering, University of Alberta, Edmonton, Alberta T6G 2V4, Canada.
Andrzej JoachimiakMidwest Center for Structural Genomics, Argonne National Laboratory, Argonne, IL 60439, USA.
Lukasz KurganElectrical and Computer Engineering, University of Alberta, Edmonton, Alberta T6G 2V4, Canada.
University of Alberta · CAArgonne National Laboratory · US

Funding

Midwest Center for Structural GenomicsU54GM094585 · NIGMS · UNIVERSITY OF CHICAGO · PI MINOR, WLADEK · 2010 to 2014
$33.7M
NIGMS NIH HHS GM094585NIGMS NIH HHS U54 GM094585
6 · The paper itself

Abstract

Structural genomics programs have developed and applied structure-determination pipelines to a wide range of protein targets, facilitating the visualization of macromolecular interactions and the understanding of their molecular and biochemical functions. The fundamental question of whether three-dimensional structures of all proteins and all functional annotations can be determined using X-ray crystallography is investigated. A first-of-its-kind large-scale analysis of crystallization propensity for all proteins encoded in 1953 fully sequenced genomes was performed. It is shown that current X-ray crystallographic knowhow combined with homology modeling can provide structures for 25% of modeling families (protein clusters for which structural models can be obtained through homology modeling), with at least one structural model produced for each Gene Ontology functional annotation. The coverage varies between superkingdoms, with 19% for eukaryotes, 35% for bacteria and 49% for archaea, and with those of viruses following the coverage values of their hosts. It is shown that the crystallization propensities of proteomes from the taxonomic superkingdoms are distinct. The use of knowledge-based target selection is shown to substantially increase the ability to produce X-ray structures. It is demonstrated that the human proteome has one of the highest attainable coverage values among eukaryotes, and GPCR membrane proteins suitable for X-ray structure determination were determined.

Indexed as

AnimalsCrystallography, X-RayDatabases, ProteinHumansProtein ConformationProteinsProteomeProteomicsReceptors, G-Protein-CoupledStructural Homology, ProteinProteinsProteomeReceptors, G-Protein-Coupledcrystallization propensityfDETECTproteome coverage

Identifiers

PMID25372670
PMCPMC4220968
OpenAlexW2170243504

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.