Crystallization and initial crystallographic characterization of the Corynebacterium glutamicum nitrilotriacetate monooxygenase component A
- Beamline Division, Pohang Accelerator Laboratory, Pohang, Kyungbuk 790-784 (Korea, Republic of)
- 21C Frontier Microbial Genomics and Applications Center, KRIBB, Daejeon 305-806 (Korea, Republic of)
- School of Life Science and Biotechnology, Kyungpook National University, Daegu 702-701 (Korea, Republic of)
The Corynebacterium glutamicum NTA monooxygenase component A protein, which plays the central role in NTA biodegradation, was crystallized. The initial X-ray crystallographic characterization is reported. 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 Å 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 Å, β = 101.94°. The asymmetric unit consists of four molecules, corresponding to a packing density of 2.3 Å{sup 3} Da{sup −1}. The structure was solved by molecular replacement. Structure refinement is in progress.
- OSTI ID:
- 22356387
- Journal Information:
- Acta Crystallographica. Section F, Vol. 62, Issue Pt 11; Other Information: PMCID: PMC2225209; PMID: 17077499; PUBLISHER-ID: en5201; OAI: oai:pubmedcentral.nih.gov:2225209; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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