Home > Publications database > Cloning, Expression, Purification and Preliminary X-ray Analysis of EstN2, a Novel Archaeal $\alpha/\beta$-Hydrolase from Candidatus Nitrososphaera Gargensis > print

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|a Kaljunen, Heidi
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245 _ _ |a Cloning, Expression, Purification and Preliminary X-ray Analysis of EstN2, a Novel Archaeal $\alpha/\beta$-Hydrolase from Candidatus Nitrososphaera Gargensis
260 _ _ |a Oxford [u.a.]
|b Blackwell
|c 2014
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500 _ _ |a (c) International Union of Crystallography. Post referee full text in progress.
520 _ _ |a EstN2 is a novel $\alpha/\beta$-hydrolase originating from the ammonia-oxidizing thaumarchaeon $\mathit{Candidatus}$ Nitrososphaera gargensis. The genome of the organism was sequenced and genes conferring putative lipolytic activity were amplified and cloned into $\mathit{Escherichia coli}$ 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 $\mathit{I2}$, with one molecule per asymmetric unit, and diffracted X-rays to 1.5 Å resolution.
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|a Mueller-Dieckmann, Jochen
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