Expression, crystallization and preliminary X-ray diffraction studies of N-carbamyl-D-amino-acid amidohydrolase from Agrobacterium radiobacter.

Hsu WH; Hsu CL; Wang TCYuan HSWang WCChien FT

首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Expression, crystallization and preliminary X-ray diffraction studies of N-carbamyl-D-amino-acid amidohydrolase from Agrobacterium radiobacter.

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Expression, crystallization and preliminary X-ray diffraction studies of N-carbamyl-D-amino-acid amidohydrolase from Agrobacterium radiobacter.

机译：表达、结晶和初步的x射线衍射研究N-carbamyl-D-amino-acid从农杆菌radiobacter酰胺水解酶。

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The Agrobacterium radiobacter CCRC 14924 N-carbamyl-D-amino-acid amidohydrolase, the enzyme used for production of D-amino acids, was overexpressed in Escherichia coli JM109. The expressed protein was crystallized by vapour diffusion using lithium sulfate as precipitant. It crystallizes in space group P21 with unit-cell parameters a = 69.8, b = 67.9 and c = 137.8 A and beta = 96.4 degrees. There are four molecules per asymmetric unit. Crystals diffract to 2.8 A resolution using a rotating-anode source at cryogenic (113 K) temperatures.

机译：农杆菌radiobacter CCRC 14924N-carbamyl-D-amino-acid酰胺水解酶,酶分子酸用于生产,在大肠杆菌JM109。表达的蛋白质被蒸发结晶扩散使用硫酸锂作为沉淀剂。它与单胞P21在空间群结晶参数= 69.8,b = 67.9和c = 137.8β= 96.4度。不对称单元。使用一个旋转阳极来源的决议低温(113 K)的温度。

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《Acta crystallographica.Section D. Biological crystallography》 |1999年第3期|694-695|共2页
作者
Hsu WH; Hsu CL; Wang TCYuan HSWang WCChien FT;
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作者单位

Institute of Molecular Biology, National Chung Hsing University, Taichung, Taiwan.;

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正文语种英语
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Amidohydrolases; Protein Conformation; CrystallographyX-ray diffractionlithium sulfatesX-raysCloningpolyacrylamide gelsCrystallizationElectrophoresis;

机译：酰胺水解酶,蛋白质构象;CrystallographyX-raydiffractionlithiumsulfatesX-raysCloningpolyacrylamidegelsCrystallizationElectrophoresis;

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Expression, crystallization and preliminary X-ray diffraction studies of N-carbamyl-D-amino-acid amidohydrolase from Agrobacterium radiobacter.

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