Evidence map›Paper›PMID 17909288›Full record

ArticleActa crystallographica. Section F, Structural biology and crystallization communications2007

Crystallization and preliminary crystallographic analysis of the ferredoxin component of carbazole 1,9a-dioxygenase from Nocardioides aromaticivorans IC177.

Kengo Inoue, Yuji Ashikawa, Yusuke Usami, Haruko Noguchi, Zui Fujimoto, Hisakazu Yamane, Hideaki Nojiri

Abstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2007. 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

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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

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

7 authors.

Kengo InoueBiotechnology Research Center, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
Yuji Ashikawa
Yusuke Usami
Haruko Noguchi
Zui Fujimoto
Hisakazu Yamane
Hideaki Nojiri

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Carbazole 1,9a-dioxygenase (CARDO) catalyzes the dihydroxylation of carbazole by angular position (C9a) carbon bonding to the imino nitrogen and its adjacent C1 carbon. CARDO consists of a terminal oxygenase component and two electron-transfer components: ferredoxin and ferredoxin reductase. The ferredoxin component of carbazole 1,9a-dioxygenase from Nocardioides aromaticivorans IC177 was crystallized at 293 K using the hanging-drop vapour-diffusion method with ammonium sulfate as the precipitant. The crystals, which were improved by macroseeding, diffract to 2.0 A resolution and belong to space group P4(1)2(1)2.

Indexed as

Bacterial ProteinsCrystallizationCrystallography, X-RayDioxygenasesFerredoxinsNocardiaceaeBacterial Proteinscarbazole 1,9a-dioxygenaseDioxygenasesFerredoxins

Identifiers

PMID17909288
PMCPMC2339720

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.