ArticleActa crystallographica. Section F, Structural biology communications2018
Bacteriophage N4 large terminase: expression, purification and X-ray crystallographic analysis.
Article in Acta crystallographica. Section F, Structural biology communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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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
2 citing papers in PubMed, 5 citations in OpenAlex.
- Article
- Genomic characterization of four novel bacteriophages infecting the clinical pathogen Klebsiella pneumoniae.DNA research : an international journal for rapid publication of reports on genes and genomes · 2021Article
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4 authors at 1 institution in 1 country.
Funding
Abstract
Genome packaging is a critical step in the assembly of dsDNA bacteriophages and is carried out by a powerful molecular motor known as the large terminase. To date, wild-type structures of only two large terminase proteins are available, and more structural information is needed to understand the genome-packaging mechanism. Towards this goal, the large and small terminase proteins from bacteriophage N4, which infects the Escherichia coli K12 strain, have been cloned, expressed and purified. The purified putative large terminase protein hydrolyzes ATP, and this is enhanced in the presence of the small terminase. The large terminase protein was crystallized using the sitting-drop vapour-diffusion method and the crystal diffracted to 2.8 Å resolution using a home X-ray source. Analysis of the X-ray diffraction data showed that the crystal belonged to space group P2
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