Evidence map›Paper›PMID 25372820›Full record

ArticleActa crystallographica. Section F, Structural biology communications2014

Overproduction, crystallization and preliminary X-ray crystallographic analysis of Escherichia coli tRNA N6-threonylcarbamoyladenosine dehydratase.

Sunmin Kim, Keon Young Kim, Jeong Kuk Park, Byung Il Lee, Yun-Gon Kim, SangYoun Park

Abstract read
PubMed Full text at PMC Publisher
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 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

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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

2 citing papers in PubMed.

  1. Review
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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

6 authors.

Sunmin KimSchool of Systems Biomedical Science, Soongsil University, Seoul 156-743, Republic of Korea.
Keon Young KimSchool of Systems Biomedical Science, Soongsil University, Seoul 156-743, Republic of Korea.
Jeong Kuk ParkSchool of Systems Biomedical Science, Soongsil University, Seoul 156-743, Republic of Korea.
Byung Il LeeBiomolecular Function Research Branch, Division of Convergence Technology, Research Institute, National Cancer Center, Goyang, Gyeonggi 410-769, Republic of Korea.
Yun-Gon KimDepartment of Chemical Engineering, Soongsil University, Seoul 156-743, Republic of Korea.
SangYoun ParkSchool of Systems Biomedical Science, Soongsil University, Seoul 156-743, Republic of Korea.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Escherichia coli tRNA N6-threonylcarbamoyladenosine dehydratase (TcdA), previously called CsdL or YgdL, was overproduced and purified from E. coli and crystallized using polyethylene glycol 3350 as a crystallizing agent. X-ray diffraction data were collected to 2.70 Å resolution under cryoconditions using synchrotron X-rays. The crystals belonged to space group P2₁, with unit-cell parameters a=65.4, b=96.8, c=83.3 Å, β=111.7°. According to the Matthews coefficient, the asymmetric unit may contain up to four subunits of the monomeric protein, with a crystal volume per protein mass (VM) of 2.12 Å3 Da(-1) and 42.1% solvent content.

Indexed as

AdenosineAmino Acid SequenceCrystallizationCrystallography, X-RayEscherichia coliEscherichia coli ProteinsMolecular Sequence DataRNA, TransferThreonine DehydrataseAdenosineEscherichia coli ProteinsN(6)-(N-threonylcarbonyl)adenosineRNA, TransferThreonine DehydrataseCsdLN6-threonylcarbamoyladenosine dehydrataseTcdAtRNA hypermodification

Identifiers

PMID25372820
PMCPMC4231855

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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.