Crystallization and initial crystallographic characterization of the Corynebacterium glutamicum nitrilotriacetate monooxygenase component A

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dc.contributor.authorK J Kim-
dc.contributor.authorSuJin Kim-
dc.contributor.authorS Lee-
dc.contributor.authorB S Kang-
dc.contributor.authorH S Lee-
dc.contributor.authorTae Kwang Oh-
dc.contributor.authorMyung Hee Kim-
dc.date.accessioned2017-04-19T09:05:31Z-
dc.date.available2017-04-19T09:05:31Z-
dc.date.issued2006-
dc.identifier.citationActa Crystallographica. Section F, Structural Biology and Crystallization Communications,62,11,1141,1143ko
dc.identifier.issn1744-3091-
dc.identifier.uri10.1107/S1744309106042072ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/7662-
dc.description.abstractSafety and environmental concerns have recently dictated the proper disposal of nitrilotriacetate (NTA). Biodegradation of NTA is initiated by NTA monooxygenase, which is composed of two proteins: component A and component B. The NTA monooxygenase component A protein from Corynebacterium glutamicum was crystallized using the sitting-drop vapour-diffusion method in the presence of ammonium sulfate as the precipitant. X-ray diffraction data were collected to a maximum resolution of 2.5 ? on a synchrotron beamline. The crystal belongs to the monoclinic space group C2, with unit-cell parameters a = 111.04, b = 98.51, c = 171.61 ?, β = 101.94°. The asymmetric unit consists of four molecules, corresponding to a packing density of 2.3 ?3 Da-1. The structure was solved by molecular replacement. Structure refinement is in progress.-
dc.publisherInt Union Crystallography-
dc.titleCrystallization and initial crystallographic characterization of the Corynebacterium glutamicum nitrilotriacetate monooxygenase component A-
dc.title.alternativeCrystallization and initial crystallographic characterization of the Corynebacterium glutamicum nitrilotriacetate monooxygenase component A-
dc.typeArticle-
dc.citation.titleActa Crystallographica Section F-Structural Biology-
dc.citation.number11-
dc.citation.endPage1143-
dc.citation.startPage1141-
dc.citation.volume62-
dc.contributor.affiliatedAuthorSuJin Kim-
dc.contributor.affiliatedAuthorTae Kwang Oh-
dc.contributor.affiliatedAuthorMyung Hee Kim-
dc.contributor.alternativeName김경진-
dc.contributor.alternativeName김수진-
dc.contributor.alternativeName이수진-
dc.contributor.alternativeName강범식-
dc.contributor.alternativeName이흥수-
dc.contributor.alternativeName오태광-
dc.contributor.alternativeName김명희-
dc.identifier.bibliographicCitationActa Crystallographica Section F-Structural Biology, vol. 62, no. 11, pp. 1141-1143-
dc.identifier.doi10.1107/S1744309106042072-
dc.subject.keywordNitrilotriacetate-
dc.subject.keywordNitrilotriacetate monooxygenase component A-
dc.subject.localNitrilotriacetate-
dc.subject.localNitrilotriacetate monooxygenase component A-
dc.description.journalClassY-
Appears in Collections:
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
Division of Biomedical Research > Microbiome Convergence Research Center > 1. Journal Articles
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