Overexpression, purification, crystallization and preliminary X-ray crystal analysis of Bacillus pallidusD-arabinose isomerase.

Overexpression, purification, crystallization and preliminary X-ray crystal analysis of Bacillus pallidusD-arabinose isomerase.
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苍白芽孢杆菌D-阿拉伯糖异构酶的过表达、纯化、结晶和初步X射线晶体分析。

DOI:
10.1107/s1744309108028352
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发表时间:
2008
期刊:
Acta crystallographica. Section F, Structural biology and crystallization communications
影响因子:
--
通讯作者:
S. Kamitori
S. Kamitori
中科院分区:
--
文献类型:
--
作者:
K. Takeda;H. Yoshida;G. Takada;K. Izumori;S. Kamitori

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相似文献

D-阿拉伯糖异构酶催化D-阿拉伯糖异构为D-核酮糖。苍白芽孢杆菌D-阿拉伯糖异构酶具有广泛的底物特异性,可以催化D-阿拉伯糖、L-岩藻糖、L-木糖、L-半乳糖和D-阿卓糖的异构化。重组B。pallidus D-阿拉伯糖异构酶的过表达、纯化和结晶。室温下用坐滴法获得了该酶的晶体,晶体属正交晶系,空间群为P2(1)2(1)2,晶胞参数a = 144.9,B = 127.9,c = 109.5。收集衍射数据至2.3 A分辨率。
D-Arabinose isomerase catalyzes the isomerization of D-arabinose to D-ribulose. Bacillus pallidus D-arabinose isomerase has broad substrate specificity and can catalyze the isomerization of D-arabinose, L-fucose, L-xylose, L-galactose and D-altrose. Recombinant B. pallidus D-arabinose isomerase was overexpressed, purified and crystallized. A crystal of the enzyme was obtained by the sitting-drop method at room temperature and belonged to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 144.9, b = 127.9, c = 109.5 A. Diffraction data were collected to 2.3 A resolution.
DOI: 10.1006/jmbi.2000.3896
发表时间: 2000-07-21
影响因子: 5.6
作者:
Korndörfer, IP;Fessner, WD;Matthews, BW
通讯作者: Matthews, BW
DOI: 10.1021/bi00172a026
发表时间: 1994-02-15
期刊: BIOCHEMISTRY
影响因子: 2.9
作者:
ALLEN, KN;LAVIE, A;RINGE, D
通讯作者: RINGE, D