Evidence map›Paper›PMID 26894670›Full record

ArticleActa crystallographica. Section D, Structural biology2016

Lessons from ten years of crystallization experiments at the SGC.

Jia Tsing Ng, Carien Dekker, Paul Reardon, Frank von Delft

Abstract read
In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Review
  2. The Starting Point for Biomolecular Crystallisation.Advances in biochemical engineering/biotechnology · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Moving beyond MARCO.PloS one · 2023
    Article
  7. Conformational changes of loops highlight a potential binding site in Rhodococcus equi VapB.Acta crystallographica. Section F, Structural biology communications · 2021
    Article
  8. Article
  9. A fully automated crystallization apparatus for small protein quantities.Acta crystallographica. Section F, Structural biology communications · 2021
    Article
  10. Review
  11. Article
  12. BLASTing away preconceptions in crystallization trials.Acta crystallographica. Section F, Structural biology communications · 2019
    Article
  13. Review
  14. Cinder: keeping crystallographers app-y.Acta crystallographica. Section F, Structural biology communications · 2018
    Article
  15. Article
  16. Article
  17. Review
  18. Gentle, fast and effective crystal soaking by acoustic dispensing.Acta crystallographica. Section D, Structural biology · 2017
    Article
  19. Guidelines for the successful generation of protein-ligand complex crystals.Acta crystallographica. Section D, Structural biology · 2017
    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

4 authors.

Jia Tsing NgStructural Genomics Consortium, University of Oxford, Roosevelt Drive, Oxford OX3 7DQ, England.
Carien DekkerCenter for Proteomic Chemistry, Novartis Institutes for Biomedical Research, CH-4002 Basel, Switzerland.
Paul ReardonSwissci AG, Industriestrasse 3, CH-6345 Neuheim, Switzerland.
Frank von DelftStructural Genomics Consortium, University of Oxford, Roosevelt Drive, Oxford OX3 7DQ, England.

Funding

Wellcome Trust
6 · The paper itself

Abstract

Although protein crystallization is generally considered more art than science and remains significantly trial-and-error, large-scale data sets hold the promise of providing general learning. Observations are presented here from retrospective analyses of the strategies actively deployed for the extensive crystallization experiments at the Oxford site of the Structural Genomics Consortium (SGC), where comprehensive annotations by SGC scientists were recorded on a customized database infrastructure. The results point to the importance of using redundancy in crystallizing conditions, specifically by varying the mixing ratios of protein sample and precipitant, as well as incubation temperatures. No meaningful difference in performance could be identified between the four most widely used sparse-matrix screens, judged by the yield of crystals leading to deposited structures; this suggests that in general any comparison of screens will be meaningless without extensive cross-testing. Where protein sample is limiting, exploring more conditions has a higher likelihood of being informative by yielding hits than does redundancy of either mixing ratio or temperature. Finally, on the logistical question of how long experiments should be stored, 98% of all crystals that led to deposited structures appeared within 30 days. Overall, these analyses serve as practical guidelines for the design of initial screening experiments for new crystallization targets.

Indexed as

CrystallizationCrystallography, X-RayHumansProteinsProteinscrystallization screening strategydata mininglarge-scale data setsredundancy of conditionssparse-matrix screens

Identifiers

PMID26894670
PMCPMC4756611

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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.