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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology Communications, 10(70), p. 1394-1397, 2014

DOI: 10.1107/s2053230x14018482

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Cloning, expression, purification and preliminary X-ray analysis of EstN2, a novel archaeal α/β-hydrolase fromCandidatusNitrososphaera gargensis

Journal article published in 2014 by Heidi Kaljunen, Jennifer Chow ORCID, Wolfgang R. Streit ORCID, Jochen Mueller-Dieckmann
This paper is available in a repository.
This paper is available in a repository.

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Abstract

EstN2 is a novel [alpha]/[beta]-hydrolase originating from the ammonia-oxidizing thaumarchaeon Candidatus Nitrososphaera gargensis. The genome of the organism was sequenced and genes conferring putative lipolytic activity were amplified and cloned into Escherichia coli as a heterologous host. Through function-based screening, esterase and lipase activity was detected. A recombinant enzyme designated EstN2 was successfully expressed, purified and crystallized. The crystals belonged to space group I2, with one molecule per asymmetric unit, and diffracted X-rays to 1.5 Å resolution.Keywords: EstN2; [alpha]/[beta]-hydrolase; Candidatus Nitrososphaera gargensis.