Expression, purification, crystallization and preliminary X- ray diffraction analysis of EtFPOX from Eupenicillium terrenum sp.

被引：7
作者：
Xing, Keke [1 ,2 ]
Gan, Weiqiong [1 ]
Jia, Minze [1 ]
Gao, Feng [1 ]
Gong, Weimin [1 ]
机构：
[1] Chinese Acad Sci, Inst Biophys, Lab Noncoding RNA, Beijing 100101, Peoples R China
[2] Chinese Acad Sci, Grad Univ, Beijing 100039, Peoples R China
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2013年 / 69卷
基金：
美国国家科学基金会;
关键词：
FRUCTOSYL-AMINE OXIDASE; ACID OXIDASE; CLONING; SITE;
D O I：
10.1107/S1744309113012128
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
The flavoenzyme fructosyl peptide oxidase (FPOX) catalyses the oxidative deglycation of fructosyl amino acids or fructosyl dipeptides to produce amino acids, glucosone and hydrogen peroxide. In this study, FPOX protein from Eupenicillium terrenum sp. (EtFPOX) was expressed in Escherichia coli and purified by Ni-affinity and gel-filtration chromatography. EtFPOX crystals were obtained using the sitting-drop vapour-diffusion method with polyethylene glycol 3350 as precipitant. X-ray diffraction data were collected to 1.90 angstrom resolution using a synchrotron-radiation source. The crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 65.6, b = 80.0, c = 83.4 angstrom, and contained one molecule in the asymmetric unit. The calculated Matthews coefficient and solvent content were 2.22 angstrom (3) Da(-1) and 44.62%, respectively.
引用
收藏
页码：666 / 668
页数：3
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