Crystallization and X-ray diffraction analysis of nylon hydrolase (NylC) from Arthrobacter sp KI72

被引：6
|
作者：
Nagai, Keisuke [1 ]
Yasuhira, Kengo [1 ]
Tanaka, Yusuke [1 ]
Kato, Dai-ichiro [1 ]
Takeo, Masahiro [1 ]
Higuchi, Yoshiki [2 ,3 ]
Negoro, Seiji [1 ]
Shibata, Naoki [2 ,3 ]
机构：
[1] Univ Hyogo, Grad Sch Engn, Dept Mat Sci & Chem, Himeji, Hyogo 6712280, Japan
[2] Univ Hyogo, Grad Sch Life Sci, Dept Life Sci, Kamigori, Hyogo 6781297, Japan
[3] RIKEN SPring 8 Ctr, Sayo, Hyogo 6795248, Japan
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2013年 / 69卷
基金：
日本学术振兴会;
关键词：
OLIGOMER DEGRADATION GENE; 6-AMINOHEXANOATE-DIMER HYDROLASE; CRYSTALLOGRAPHIC ANALYSIS; PLASMID POAD2; CARBOXYLESTERASE; ENZYMES;
D O I：
10.1107/S1744309113024263
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Nylon hydrolase (NylC) encoded by Arthrobacter plasmid pOAD2 (NylC(p2)) was expressed in Escherichia coli JM109 and purified by ammonium sulfate fractionation, anion-exchange column chromatography and gel-filtration chromatography. NylC(p2) was crystallized by the sitting-drop vapour-diffusion method with ammonium sulfate as a precipitant in 0.1 M HEPES buffer pH 7.5 containing 0.2 M NaCl and 25% glycerol. Diffraction data were collected from the native crystal to a resolution of 1.60 angstrom. The obtained crystal was spindle shaped and belonged to the C-centred orthorhombic space group C222(1), with unit-cell parameters a = 70.84, b = 144.90, c = 129.05 angstrom. A rotation and translation search gave one clear solution containing two molecules per asymmetric unit.
引用
收藏
页码：1151 / 1154
页数：4
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