Evidence map›Paper›PMID 40170961›Full record

ArticleJournal of applied crystallography2025

A generic cross-seeding approach to protein crystallization.

Ido Caspy, Shan Tang, Dom Bellini, Fabrice Gorrec

Abstract read
In one paragraph

Article in Journal of applied crystallography, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Preparing for successful protein crystallization experiments.Acta crystallographica. Section F, Structural biology communications · 2025
    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

4 authors.

Ido CaspyMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, CambridgeCB2 0QH, United Kingdom.ORCID https://orcid.org/0000-0003-1981-1017
Shan TangDivision of Life Sciences and Medicine University of Science and Technology of China Hefei Anhui230001 People's Republic of China.
Dom BelliniMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, CambridgeCB2 0QH, United Kingdom.
Fabrice GorrecMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, CambridgeCB2 0QH, United Kingdom.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Obtaining diffraction-quality crystals is often the rate-limiting step during structure determination of biological macromolecules by X-ray crystallography. To address this problem, we investigated a cross-seeding approach with a mixture integrating a heterogeneous set of protein crystal fragments to be used as generic seeds. The fragments are nanometre-sized templates chosen to promote crystal nucleation of protein samples unrelated to the proteins forming the seeds. An atypical crystal form of the human serine hydrolase retinoblastoma binding protein 9 was obtained by adding the mixture to the protein sample before performing standard crystallization assays. The structure was solved by X-ray crystallography at 1.4 Å resolution. Follow-up experiments showed that crystal fragments of α-amylase were critical components in this particular result. The limitations and future applications of our experimental developments are discussed.

Indexed as

cross-seedingmacromolecular crystallizationnucleationprotein crystalsX-ray crystallography

Identifiers

PMID40170961
PMCPMC11957411

What OpenQuestion holds

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Registered trials

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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.