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Article

Crystallization and preliminary crystallographic analysis of an Escherichia coli-selected mutant of the nuclease domain of the metallonuclease colicin E7.

Acta crystallographica. Section F, Structural biology and crystallization communications - 1 May 2013

Czene Anikó, Tóth Eszter, Gyurcsik Béla, Otten Harm, Poulsen Jens Christian N, Lo Leggio Leila, Larsen Sine, Christensen Hans E M, Nagata Kyosuke

Abstract excerpt

The metallonuclease colicin E7 is a member of the HNH family of endonucleases. It serves as a bacterial toxin in Escherichia coli, protecting the host cell from other related bacteria and bacteriophages by degradation of their chromosomal DNA under environmental stress. Its cell-killing activity is attributed to the nonspecific nuclease domain (NColE7), which possesses the catalytic ββα-type metal ion-binding HNH...

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Identifiers

PMID: 23695575
DOI: 10.1107/S1744309113008233
PMCID: PMC3660899

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Crystallization and preliminary crystallographic analysis of an Escherichia coli-selected mutant of the nuclease domain of the metallonuclease colicin E7.PMID 23695575Read ↗

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