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

页码：1151 / 1154

页数：4

共 40 条

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