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    National Tsing Hua University Institutional Repository > 生命科學院  > 生命科學系 > 期刊論文 >  Expression, crystallization and preliminary X-ray diffraction studies of N-carbamyl-D-amino-acid amidohydrolase from Agrobacterium radiobacter


    Please use this identifier to cite or link to this item: http://nthur.lib.nthu.edu.tw/dspace/handle/987654321/48416


    Title: Expression, crystallization and preliminary X-ray diffraction studies of N-carbamyl-D-amino-acid amidohydrolase from Agrobacterium radiobacter
    Authors: Hsu WH;Chien FT;Hsu CL;Wang TC;Yuan HS;Wang WC
    教師: 王雯靜
    Date: 1999
    Publisher: International Union of Crystallography
    Relation: ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY,International Union of Crystallography,Volume 55,MAR 1999,Pages 694-695
    Keywords: purification
    Abstract: 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 P2(1) with unit-cell parameters cr = 69.8, b = 67.9 and c = 137.8 Angstrom and beta = 96.4 degrees. There are four molecules per asymmetric unit. Crystals diffract to 2.8 Angstrom resolution using a rotating-anode source at cryogenic (113 K) temperatures.
    URI: http://www.iucr.org/
    http://nthur.lib.nthu.edu.tw/dspace/handle/987654321/48416
    Appears in Collections:[生命科學系] 期刊論文

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