Evidence map›Paper›PMID 19342782›Full record

ArticleActa crystallographica. Section F, Structural biology and crystallization communications2009

Overexpression, purification and crystallization of a thermostable DNA ligase from the archaeon Thermococcus sp. 1519.

E Y Bezsudnova, M V Kovalchuk, A V Mardanov, K M Poliakov, V O Popov, N V Ravin, K G Skryabin, V A Smagin, T N Stekhanova, T V Tikhonova

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.4field-weighted citation impact, top 38% 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

4 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Review
  3. ATP-dependent DNA ligase from Thermococcus sp. 1519 displays a new arrangement of the OB-fold domain.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012
    Article
  4. 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

10 authors at 5 institutions in 1 country.

E Y BezsudnovaBach Institute of Biochemistry RAS, Leninsky Prospect 33, 119071 Moscow, Russia. eubez@yandex.ru
M V Kovalchuk
A V Mardanov
K M Poliakov
V O Popov
N V Ravin
K G Skryabin
V A Smagin
T N Stekhanova
T V Tikhonova
Bioengineering Center · RUA N Bach Institute of Biochemistry · RUEngelhardt Institute of Molecular Biology · RUKurchatov Institute · RUYandex (Russia) · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DNA ligases catalyze the sealing of 5'-phosphate and 3'-hydroxyl termini at single-strand breaks in double-stranded DNA and their function is essential to maintain the integrity of the genome in DNA metabolism. An ATP-dependent DNA ligase from the archaeon Thermococcus sp. 1519 was overexpressed, purified and crystallized. Crystals were obtained using the hanging-drop vapour-diffusion method employing 35%(v/v) Tacsimate pH 7.0 as a precipitant and diffracted X-rays to 3.09 A resolution. They belonged to space group P4(1)2(1)2, with unit-cell parameters a = b = 79.7, c = 182.6 A.

Indexed as

TemperatureCrystallizationCrystallography, X-RayDNA LigasesElectrophoresis, Polyacrylamide GelEnzyme StabilityRecombinant ProteinsThermococcusDNA LigasesRecombinant Proteins

Identifiers

PMID19342782
PMCPMC2664762
OpenAlexW1970088293

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.