Evidence map›Paper›PMID 24699746›Full record

ArticleActa crystallographica. Section F, Structural biology communications2014

Cloning, crystallization and preliminary X-ray diffraction analysis of an intact DNA methyltransferase of a type I restriction-modification enzyme from Vibrio vulnificus.

Ly Huynh Thi Yen, Suk-Youl Park, Jeong-Sun Kim

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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 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact, top 93% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. 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

3 authors at 1 institution in 1 country.

Ly Huynh Thi YenDepartment of Chemistry, Chonnam National University, Gwangju 500-757, Republic of Korea.
Suk-Youl ParkDepartment of Chemistry, Chonnam National University, Gwangju 500-757, Republic of Korea.
Jeong-Sun KimDepartment of Chemistry, Chonnam National University, Gwangju 500-757, Republic of Korea.
Chonnam National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Independently of the restriction (HsdR) subunit, the specificity (HsdS) and methylation (HsdM) subunits interact with each other, and function as a methyltransferase in type I restriction-modification systems. A single gene that combines the HsdS and HsdM subunits in Vibrio vulnificus YJ016 was expressed and purified. A crystal suitable for X-ray diffraction was obtained from 25%(w/v) polyethylene glycol monomethylether 5000, 0.1 M HEPES pH 8.0, 0.2 M ammonium sulfate at 291 K by hanging-drop vapour diffusion. Diffraction data were collected to a resolution of 2.31 Å using synchrotron radiation. The crystal belonged to the primitive monoclinic space group P21, with unit-cell parameters a = 93.25, b = 133.04, c = 121.49 Å, β = 109.7°. With four molecules in the asymmetric unit, the crystal volume per unit protein weight was 2.61 Å(3) Da(-1), corresponding to a solvent content of 53%.

Indexed as

Cloning, MolecularAmino Acid SequenceCrystallizationCrystallography, X-RayDeoxyribonucleases, Type I Site-SpecificDNAMethylationMolecular Sequence DataProtein SubunitsSequence Homology, Amino AcidSynchrotronsVibrio vulnificusDeoxyribonucleases, Type I Site-SpecificDNAProtein SubunitsDNA methyltransferasesmethylation subunitspecificity subunittype I restriction and modification

Identifiers

PMID24699746
PMCPMC3976070
OpenAlexW2028958204

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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.