title: Expression, purification, crystallization and preliminary X-ray diffraction analysis of EtFPOX from Eupenicillium terrenum sp.
abstract: 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 Å 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 Å, and contained one molecule in the asymmetric unit. The calculated Matthews coefficient and solvent content were 2.22 Å(3) Da(-1) and 44.62%, respectively.
authors.affiliation: Laboratory of Noncoding RNA, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing 100101, People's Republic of China.
authors.forename: Keke
authors.initials: K
authors.lastname: Xing
authors.forename: Weiqiong
authors.initials: W
authors.lastname: Gan
authors.forename: Minze
authors.initials: M
authors.lastname: Jia
authors.forename: Feng
authors.initials: F
authors.lastname: Gao
authors.forename: Weimin
authors.initials: W
authors.lastname: Gong
mesh_terms: D000594:Amino Acid Oxidoreductases / Q000096:biosynthesis* / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D055324:Eupenicillium / Q000201:enzymology*; D005656:Fungal Proteins / Q000096:biosynthesis* / Q000737:chemistry* / Q000302:isolation & purification; D015966:Gene Expression Regulation, Fungal; D014961:X-Ray Diffraction
chemical_list: D005656:Fungal Proteins; D000594:Amino Acid Oxidoreductases; C520096:fructosyl-peptide oxidase
keywords: EtFPOX; Eupenicillium terrenum sp.; FPOX