Evidence map›Paper›PMID 16511087›Full record

ArticleActa crystallographica. Section F, Structural biology and crystallization communications2005

Crystallization and preliminary crystallographic analysis of a flavoprotein NADH oxidase from Lactobacillus brevis.

Mutlu Kuzu, Karsten Niefind, Werner Hummel, Dietmar Schomburg

Open access · greenAbstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2005. 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
0.3field-weighted citation impact, top 44% 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, 6 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

4 authors at 2 institutions in 1 country.

Mutlu KuzuInstitute of Molecular Enzyme Technology, Heinrich Heine University Düsseldorf, Research Centre Jülich, 52426 Jülich, Germany.
Karsten Niefind
Werner Hummel
Dietmar Schomburg
Heinrich Heine University Düsseldorf · DEUniversity of Cologne · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

NADH oxidase (NOX) from Lactobacillus brevis is a homotetrameric flavoenzyme composed of 450 amino acids per subunit. The molecular weight of each monomer is 48.8 kDa. The enzyme catalyzes the oxidation of two equivalents of NADH and reduces one equivalent of oxygen to yield two equivalents of water, without releasing hydrogen peroxide after the reduction of the first equivalent of NADH. Crystals of this protein were grown in the presence of 34% polyethylene glycol monomethyl ether 2000, 0.1 M sodium acetate and 0.2 M ammonium sulfate at pH 5.4. They belong to the tetragonal space group P4(3)2(1)2, with unit-cell parameters a = 74.8, b = 95.7, c = 116.9 A, alpha = gamma = 90, beta = 103.8 degrees. The current diffraction limit is 4.0 A. The self-rotation function of the native data set is consistent with a NOX tetramer in the asymmetric unit.

Indexed as

CrystallizationCrystallography, X-RayEscherichia coliFlavoproteinsLevilactobacillus brevisMultienzyme ComplexesNADH, NADPH OxidoreductasesRecombinant ProteinsFlavoproteinsMultienzyme ComplexesNADH, NADPH OxidoreductasesNADH oxidaseRecombinant Proteins

Identifiers

PMID16511087
PMCPMC1952304
OpenAlexW2050351304

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.