Evidence map›Paper›PMID 25195878›Full record

ArticleActa crystallographica. Section F, Structural biology communications2014

Microseed matrix screening for optimization in protein crystallization: what have we learned?

Allan D'Arcy, Terese Bergfors, Sandra W Cowan-Jacob, May Marsh

Abstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing 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

71 citing papers in PubMed.

  1. Towards routine accurate electron-density studies of biological macromolecules.Acta crystallographica. Section D, Structural biology · 2026
    Article
  2. Crystal Structure and Conformational Dynamics of N─N Bond-Forming Piperazate Synthase.Chembiochem : a European journal of chemical biology · 2026
    Article
  3. Crystallization and 1.6 Å resolution crystal structure of an acylated GLP-1/GIP analogue peptide.Acta crystallographica. Section F, Structural biology communications · 2026
    Article
  4. Article
  5. Molecular structure and nickel-binding capacity of Proteus mirabilis UreE.Acta crystallographica. Section D, Structural biology · 2026
    Article
  6. Article
  7. The Starting Point for Biomolecular Crystallisation.Advances in biochemical engineering/biotechnology · 2026
    Review
  8. Biomolecular Crystallisation Through Soft Templates and Seeding.Advances in biochemical engineering/biotechnology · 2026
    Review
  9. Alternative Strategies to Promote Biomolecule Nucleation.Advances in biochemical engineering/biotechnology · 2026
    Review
  10. Article
  11. Preparing for successful protein crystallization experiments.Acta crystallographica. Section F, Structural biology communications · 2025
    Article
  12. Article
  13. Article
  14. Review
  15. A generic cross-seeding approach to protein crystallization.Journal of applied crystallography · 2025
    Article
  16. Article
  17. Article
  18. Expansion of the diversity of dispersin scaffolds.Acta crystallographica. Section D, Structural biology · 2025
    Article
  19. Article
  20. Article

11 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

4 authors.

Allan D'ArcyActelion Pharmaceuticals Ltd, Basel, Switzerland.
Terese BergforsDepartment of Cell and Molecular Biology, Uppsala University, Uppsala, Sweden.
Sandra W Cowan-JacobNovartis Institutes for Biomedical Research, Novartis Campus, 4056 Basel, Switzerland.
May MarshSwiss Light Source, Paul Scherrer Institute, 5232 Villigen PSI, Switzerland.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein crystals obtained in initial screens typically require optimization before they are of X-ray diffraction quality. Seeding is one such optimization method. In classical seeding experiments, the seed crystals are put into new, albeit similar, conditions. The past decade has seen the emergence of an alternative seeding strategy: microseed matrix screening (MMS). In this strategy, the seed crystals are transferred into conditions unrelated to the seed source. Examples of MMS applications from in-house projects and the literature include the generation of multiple crystal forms and different space groups, better diffracting crystals and crystallization of previously uncrystallizable targets. MMS can be implemented robotically, making it a viable option for drug-discovery programs. In conclusion, MMS is a simple, time- and cost-efficient optimization method that is applicable to many recalcitrant crystallization problems.

Indexed as

CrystallizationCrystallography, X-RayModels, MolecularProteinsProteinscrystallizationmicroseed matrix screeningoptimization

Identifiers

PMID25195878
PMCPMC4157405

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.