Evidence map›Paper›PMID 25005103›Full record

ArticleActa crystallographica. Section F, Structural biology communications2014

Purification, crystallization and room-temperature X-ray diffraction of inositol dehydrogenase LcIDH2 from Lactobacillus casei BL23.

Drew Bertwistle, Linda Vogt, Hari Babu Aamudalapalli, David R J Palmer, David A R Sanders

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 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. 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

5 authors.

Drew BertwistleDepartment of Chemistry, University of Saskatchewan, 110 Science Place, Saskatoon SK S7N 5C9, Canada.
Linda VogtDepartment of Chemistry, University of Saskatchewan, 110 Science Place, Saskatoon SK S7N 5C9, Canada.
Hari Babu AamudalapalliDepartment of Chemistry, University of Saskatchewan, 110 Science Place, Saskatoon SK S7N 5C9, Canada.
David R J PalmerDepartment of Chemistry, University of Saskatchewan, 110 Science Place, Saskatoon SK S7N 5C9, Canada.
David A R SandersDepartment of Chemistry, University of Saskatchewan, 110 Science Place, Saskatoon SK S7N 5C9, Canada.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lactobacillus casei BL23 contains two genes, iolG1 and iolG2, homologous with inositol dehydrogenase encoding genes from many bacteria. Inositol dehydrogenase catalyzes the oxidation of inositol with concomitant reduction of NAD+. The protein encoded by iolG2, LcIDH2, has been purified to homogeneity, crystallized and cryoprotected for diffraction at 77 K. The crystals had a high mosaicity and poor processing statistics. Subsequent diffraction measurements were performed without cryoprotectant at room temperature. These crystals were radiation-resistant and a full diffraction data set was collected at room temperature to 1.6 Å resolution.

Indexed as

Amino Acid SequenceBacterial ProteinsCloning, MolecularCrystallizationCrystallography, X-RayEscherichia coliGene ExpressionLacticaseibacillus caseiMolecular Sequence DataRecombinant ProteinsSequence AlignmentSequence Homology, Amino AcidSugar Alcohol DehydrogenasesBacterial Proteinsmyo-inositol 2-dehydrogenaseRecombinant ProteinsSugar Alcohol Dehydrogenasesinositol dehydrogenaseLactobacillus casei BL23

Identifiers

PMID25005103
PMCPMC4089546

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.