Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/67779
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dc.contributor.authorHsu, W.H.en_US
dc.contributor.authorChien, F.T.en_US
dc.contributor.authorHsu, C.L.en_US
dc.contributor.authorWang, T.C.en_US
dc.contributor.authorYuan, H.S.en_US
dc.contributor.authorWang, W.C.en_US
dc.date1999zh_TW
dc.date.accessioned2014-06-11T05:55:40Z-
dc.date.available2014-06-11T05:55:40Z-
dc.identifier.issn0907-4449zh_TW
dc.identifier.urihttp://hdl.handle.net/11455/67779-
dc.description.abstractThe 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.en_US
dc.language.isoen_USzh_TW
dc.relationActa Crystallographica Section D-Biological Crystallographyen_US
dc.relation.ispartofseriesActa Crystallographica Section D-Biological Crystallography, Volume 55, Page(s) 694-695.en_US
dc.relation.urihttp://dx.doi.org/10.1107/s090744499801525xen_US
dc.subjectpurificationen_US
dc.titleExpression, crystallization and preliminary X-ray diffraction studies of N-carbamyl-D-amino-acid amidohydrolase from Agrobacterium radiobacteren_US
dc.typeJournal Articlezh_TW
dc.identifier.doi10.1107/s090744499801525xzh_TW
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