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从海洋微生物宏基因组中纯化、结晶及重组Lac15的初步晶体学分析

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

作者信息

Ge Honghua, Xu Peisong, Xu Ying, Fang Zemin, Xiao Yazhong

机构信息

Modern Experiment Technology Center and School of Life Sciences, Anhui University, Hefei, People's Republic of China.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Aug 1;67(Pt 8):956-8. doi: 10.1107/S1744309111024912. Epub 2011 Jul 27.

DOI:10.1107/S1744309111024912
PMID:21821904
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3151137/
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, β = 112.10°.

摘要

漆酶是蓝色多铜氧化酶家族的成员,能够氧化多种芳香族化合物。最近从中国南海海洋微生物宏基因组中获得了一种新的细菌漆酶(Lac15)并对其进行了表征。在这项工作中,重组Lac15在大肠杆菌中过量表达,采用悬滴气相扩散法进行纯化和结晶。收集到了分辨率为2.2 Å的X射线衍射数据集。该晶体属于空间群C121,晶胞参数为a = 123.41、b = 91.36、c = 86.157 Å,β = 112.10°。

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