ArticleActa crystallographica. Section F, Structural biology and crystallization communications2012
Cloning, expression, crystallization and preliminary X-ray crystallographic analysis of aspartyl aminopeptidase from the apeB gene of Pseudomonas aeruginosa.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 1 paper.
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.
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Who cites it
1 citing paper in PubMed, 2 citations in OpenAlex.
- Cloning, expression, crystallization and preliminary X-ray crystallographic analysis of aspartyl aminopeptidase from the apeB gene of Pseudomonas aeruginosa. Retraction.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
Corrections and comments
- Retraction · 2012-11-01Notice - Limited or No Information · · AJA 1/2/2017
- Retracted
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aminopeptidases (APs) are a group of exopeptidases that catalyze the removal of amino acids from the N-termini of proteins and peptides. The APs are ubiquitous in nature and are of critical biological and medical importance because of their key role in protein degradation. Pseudomonas aeruginosa aspartyl aminopeptidase (PaAAP), which is encoded by the apeB gene, was expressed in Escherichia coli, purified and crystallized using the microbatch method. A preliminary structural study has been performed using the X-ray crystallographic method. The PaAAP crystal diffracted to 2.0 Å resolution and belonged to the rhombohedral space group H3, with unit-cell parameters a = b = 133.6, c = 321.2. The unit-cell volume of the crystal is compatible with the presence of four monomers in the asymmetric unit, with a corresponding Matthews coefficient V(M) of 2.95 Å(3) Da(-1) and a solvent content of 58.3%.
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