Evidence map›Paper›PMID 26174163›Full record

ArticleProtein science : a publication of the Protein Society2015

Structure of a designed tetrahedral protein assembly variant engineered to have improved soluble expression.

Jacob B Bale, Rachel U Park, Yuxi Liu, Shane Gonen, Tamir Gonen, Duilio Cascio, Neil P King, Todd O Yeates, David Baker

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Protein Assembly by Design.Chemical reviews · 2021
    Review
  9. Article
  10. A fragment-based protein interface design algorithm for symmetric assemblies.Protein engineering, design & selection : PEDS · 2021
    Article
  11. Article
  12. Near-atomic cryo-EM imaging of a small protein displayed on a designed scaffolding system.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  13. The 2017 Keystone Symposium on HIV Vaccines.Human vaccines & immunotherapeutics · 2017
    Article
  14. Article
  15. 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

9 authors.

Jacob B BaleDepartment of Biochemistry, University of Washington, Seattle, Washington, 98195.
Rachel U ParkDepartment of Biochemistry, University of Washington, Seattle, Washington, 98195.
Yuxi LiuDepartment of Chemistry and Biochemistry, UCLA, Los Angeles, California, 90095.
Shane GonenDepartment of Biochemistry, University of Washington, Seattle, Washington, 98195.
Tamir GonenJanelia Research Campus, Howard Hughes Medical Institute, Ashburn, Virginia, 20147.
Duilio CascioInstitute for Genomics and Proteomics, UCLA-DOE, Los Angeles, California, 90095.
Neil P KingDepartment of Biochemistry, University of Washington, Seattle, Washington, 98195.
Todd O YeatesDepartment of Chemistry and Biochemistry, UCLA, Los Angeles, California, 90095.
David BakerDepartment of Biochemistry, University of Washington, Seattle, Washington, 98195.

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

We recently reported the development of a computational method for the design of coassembling multicomponent protein nanomaterials. While four such materials were validated at high-resolution by X-ray crystallography, low yield of soluble protein prevented X-ray structure determination of a fifth designed material, T33-09. Here we report the design and crystal structure of T33-31, a variant of T33-09 with improved soluble yield resulting from redesign efforts focused on mutating solvent-exposed side chains to charged amino acids. The structure is found to match the computational design model with atomic-level accuracy, providing further validation of the design approach and demonstrating a simple and potentially general means of improving the yield of designed protein nanomaterials.

Indexed as

Gene ExpressionGenetic VariationProtein EngineeringComputer SimulationCrystallography, X-RayElectrophoresis, Polyacrylamide GelProteinsSolubilityProteinscoassemblycomputational protein designcrystal structurenanomaterialsolubilitysymmetrytetrahedral

Identifiers

PMID26174163
PMCPMC4594668

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.