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- Crystallization and initial crystallographic characterization of the Corynebacterium glutamicum nitrilotriacetate monooxygenase component A
- K J Kim; SuJin Kim; S Lee; B S Kang; H S Lee; Tae Kwang Oh; Myung Hee Kim
- Bibliographic Citation
- Acta Crystallographica Section F-Structural Biology, vol. 62, no. 11, pp. 1141-1143
- Publication Year
- Safety 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.
- NitrilotriacetateNitrilotriacetate monooxygenase component A
- Int Union Crystallography
- 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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