Evidence map›Paper›PMID 12824478›Full record

ReviewProtein science : a publication of the Protein Society2003

Crystal structures of fusion proteins with large-affinity tags.

Douglas R Smyth, Marek K Mrozkiewicz, William J McGrath, Pawel Listwan, Bostjan Kobe

Abstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers.

0numbers the graph read from it
0cells of the map it votes in
103citing 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

103 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Preparing for successful protein crystallization experiments.Acta crystallographica. Section F, Structural biology communications · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Tagging Recombinant Proteins to Enhance Solubility and Aid Purification.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. The Effect of Recombinant Tags onPlants (Basel, Switzerland) · 2020
    Article
  19. Article
  20. Review

43 more citing papers are in PubMed but not listed here.

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.

Douglas R SmythDepartment of Biochemistry and Molecular Biology, Institute for Molecular Bioscience, and Special Research Centre for Functional and Applied Genomics, University of Queensland, St Lucia, Queensland 4072, Australia.
Marek K Mrozkiewicz
William J McGrath
Pawel Listwan
Bostjan Kobe

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The fusion of a protein of interest to a large-affinity tag, such as the maltose-binding protein (MBP), thioredoxin (TRX), or glutathione-S-transferase (GST), can be advantageous in terms of increased expression, enhanced solubility, protection from proteolysis, improved folding, and protein purification via affinity chromatography. Unfortunately, crystal growth is hindered by the conformational heterogeneity induced by the fusion tag, requiring that the tag is removed by a potentially problematic cleavage step. The first three crystal structures of fusion proteins with large-affinity tags have been reported recently. All three structures used a novel strategy to rigidly fuse the protein of interest to MBP via a short three- to five-amino acid spacer. This strategy has the potential to aid structure determination of proteins that present particular experimental challenges and are not conducive to more conventional crystallization strategies (e.g., membrane proteins). Structural genomics initiatives may also benefit from this approach as a way to crystallize problematic proteins of significant interest.

Indexed as

Protein ConformationAffinity LabelsCarrier ProteinsCrystallography, X-RayDimerizationGenomicsGlutathione TransferaseMaltose-Binding ProteinsMembrane ProteinsRecombinant Fusion ProteinsThioredoxinsAffinity LabelsCarrier ProteinsGlutathione TransferaseMaltose-Binding ProteinsMembrane ProteinsRecombinant Fusion ProteinsThioredoxins

Identifiers

PMID12824478
PMCPMC2323919

What OpenQuestion holds

Textmetadata
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.