Evidence map›Paper›PMID 25090252›Full record

ArticlePloS one2014

Rapid purification of recombinant histones.

Henrike Klinker, Caroline Haas, Nadine Harrer, Peter B Becker, Felix Mueller-Planitz

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
1.3field-weighted citation impact, top 21% of its field
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

36 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
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  4. Remodeling of Individual Nucleosomes in Nucleosome Arrays.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  5. ISWI catalyzes nucleosome sliding in condensed nucleosome arrays.Nature structural & molecular biology · 2024
    Article
  6. Structure of the human TIP60 complex.Nature communications · 2024
    Article
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  12. ISWI catalyzes nucleosome sliding in condensed nucleosome arrays.bioRxiv : the preprint server for biology · 2023
    Article
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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 at 2 institutions in 1 country.

Henrike KlinkerMolecular Biology Unit, Adolf-Butenandt-Institute, Ludwig-Maximilians-Universität München, Munich, Germany; Center for Integrated Protein Science Munich, Germany.
Caroline HaasDepartment of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany; Gene Center, Ludwig-Maximilians-Universität München, Munich, Germany.
Nadine HarrerMolecular Biology Unit, Adolf-Butenandt-Institute, Ludwig-Maximilians-Universität München, Munich, Germany.
Peter B BeckerMolecular Biology Unit, Adolf-Butenandt-Institute, Ludwig-Maximilians-Universität München, Munich, Germany; Center for Integrated Protein Science Munich, Germany.
Felix Mueller-PlanitzMolecular Biology Unit, Adolf-Butenandt-Institute, Ludwig-Maximilians-Universität München, Munich, Germany.
Ludwig-Maximilians-Universität München · DECenter for Integrated Protein Science Munich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The development of methods to assemble nucleosomes from recombinant histones decades ago has transformed chromatin research. Nevertheless, nucleosome reconstitution remains time consuming to this day, not least because the four individual histones must be purified first. Here, we present a streamlined purification protocol of recombinant histones from bacteria. We termed this method "rapid histone purification" (RHP) as it circumvents isolation of inclusion bodies and thereby cuts out the most time-consuming step of traditional purification protocols. Instead of inclusion body isolation, whole cell extracts are prepared under strongly denaturing conditions that directly solubilize inclusion bodies. By ion exchange chromatography, the histones are purified from the extracts. The protocol has been successfully applied to all four canonical Drosophila and human histones. RHP histones and histones that were purified from isolated inclusion bodies had similar purities. The different purification strategies also did not impact the quality of octamers reconstituted from these histones. We expect that the RHP protocol can be readily applied to the purification of canonical histones from other species as well as the numerous histone variants.

Indexed as

AnimalsChromatography, Ion ExchangeDrosophila melanogasterDrosophila ProteinsEscherichia coliGene ExpressionHistonesHumansMolecular WeightProtein DenaturationProtein RefoldingRecombinant ProteinsSolid Phase ExtractionDrosophila ProteinsHistonesRecombinant Proteins

Identifiers

PMID25090252
PMCPMC4121265
OpenAlexW1994333151

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.