Journal Article

PUBDB-2015-01329

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Cloning, Expression, Purification and Preliminary X-ray Analysis of EstN2, a Novel Archaeal $\alpha/\beta$-Hydrolase from Candidatus Nitrososphaera Gargensis

Kaljunen, H.>Extern*EMBL* ; Chow, J. ; Streit, W. R. ; Mueller-Dieckmann, J. (Corresponding author)

2014
Blackwell Oxford [u.a.]

This record in other databases:        

Please use a persistent id in citations: doi:10.1107/S2053230X14018482

Abstract: 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.

Note: (c) International Union of Crystallography. Post referee full text in progress.

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Contributing Institute(s):

1. EMBL (EMBL)

Research Program(s):

1. PETRA Beamline P14 (POF2-54G14) (POF2-54G14)

Experiment(s):

1. PETRA Beamline P14 (PETRA III)

Appears in the scientific report 2014

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Database coverage:
; BIOSIS Previews ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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