Evidence map›Paper›PMID 20177794›Full record

ArticleJournal of structural and functional genomics2010

Predicting protein crystallization propensity from protein sequence.

György Babnigg, Andrzej Joachimiak

Abstract read
In one paragraph

Article in Journal of structural and functional genomics, 2010. 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. Article
  2. Data collection from crystals grown in microfluidic droplets.Acta crystallographica. Section D, Structural biology · 2022
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Databases, Repositories, and Other Data Resources in Structural Biology.Methods in molecular biology (Clifton, N.J.) · 2017
    Review
  8. Review
  9. Computational crystallization.Archives of biochemistry and biophysics · 2016
    Review
  10. Article
  11. Analysis of crystallization data in the Protein Data Bank.Acta crystallographica. Section F, Structural biology communications · 2015
    Article
  12. Covering complete proteomes with X-ray structures: a current snapshot.Acta crystallographica. Section D, Biological crystallography · 2014
    Article
  13. Improving the chances of successful protein structure determination with a random forest classifier.Acta crystallographica. Section D, Biological crystallography · 2014
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

2 authors.

György BabniggMidwest Center for Structural Genomics, Biosciences Division, Argonne National Laboratory, 9700 S Cass Ave., Argonne, IL 60439, USA. gbabnigg@anl.gov
Andrzej Joachimiak

Funding

The Midwest Center for Structural GenomicsU54GM074942 · NIGMS · UNIVERSITY OF CHICAGO · PI JOACHIMIAK, ANDRZEJ · 2005 to 2009
$51.0M
NIGMS NIH HHS GM074942NIGMS NIH HHS U54 GM074942
6 · The paper itself

Abstract

The high-throughput structure determination pipelines developed by structural genomics programs offer a unique opportunity for data mining. One important question is how protein properties derived from a primary sequence correlate with the protein's propensity to yield X-ray quality crystals (crystallizability) and 3D X-ray structures. A set of protein properties were computed for over 1,300 proteins that expressed well but were insoluble, and for approximately 720 unique proteins that resulted in X-ray structures. The correlation of the protein's iso-electric point and grand average hydropathy (GRAVY) with crystallizability was analyzed for full length and domain constructs of protein targets. In a second step, several additional properties that can be calculated from the protein sequence were added and evaluated. Using statistical analyses we have identified a set of the attributes correlating with a protein's propensity to crystallize and implemented a Support Vector Machine (SVM) classifier based on these. We have created applications to analyze and provide optimal boundary information for query sequences and to visualize the data. These tools are available via the web site http://bioinformatics.anl.gov/cgi-bin/tools/pdpredictor .

Indexed as

Amino Acid SequenceComputational BiologyCrystallizationData MiningProteinsX-RaysProteins

Identifiers

PMID20177794
PMCPMC3366497

What OpenQuestion holds

Textmetadata
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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.