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Purification, crystallization and preliminary crystallographic analysis of recombinant Lac15 from a marine microbial metagenome.


ABSTRACT: Laccases are members of the blue multi-copper oxidase family that can oxidize a wide range of aromatic compounds. A new bacterial laccase (Lac15) has recently been obtained from a marine microbial metagenome from the South China Sea and characterized. In this work, recombinant Lac15 was overexpressed in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. An X-ray diffraction data set was collected to 2.2?Å resolution. The crystal belonged to space group C121, with unit-cell parameters a = 123.41, b = 91.36, c = 86.157?Å, ? = 112.10°.

SUBMITTER: Ge H 

PROVIDER: S-EPMC3151137 | biostudies-literature | 2011 Aug

REPOSITORIES: biostudies-literature

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Purification, crystallization and preliminary crystallographic analysis of recombinant Lac15 from a marine microbial metagenome.

Ge Honghua H   Xu Peisong P   Xu Ying Y   Fang Zemin Z   Xiao Yazhong Y  

Acta crystallographica. Section F, Structural biology and crystallization communications 20110727 Pt 8


Laccases are members of the blue multi-copper oxidase family that can oxidize a wide range of aromatic compounds. A new bacterial laccase (Lac15) has recently been obtained from a marine microbial metagenome from the South China Sea and characterized. In this work, recombinant Lac15 was overexpressed in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. An X-ray diffraction data set was collected to 2.2 Å resolution. The crystal belonged to space group C1  ...[more]

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