상세 정보

underline
Metadata Downloads : dc(xml) or Excel
Cited 0 time in scopus ci

Title 

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

Authors 

K J KimSuJin KimS LeeB S KangH S LeeTae Kwang OhMyung Hee Kim

Publisher 

International Union of Crystallography

Issue Date 

2006

Citation 

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, vol. 62, no. 11, pp. 1141-1143

Keywords 

nitrilotriacetatenitrilotriacetate monooxygenase component Abacterial proteinmixed function oxidasenitrilotriacetate monooxygenasecorynebacteriumcrystallizationgel chromatographyisolation and purificationmetabolism

Abstract 

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.

Citation 

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, 62(11): 1141-1143

ISSN 

1744-3091

Link 

http://dx.doi.org/10.1107/S1744309106042072

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


Files in This Item: SizeFormat
6703.pdf175KbAdobe PDF
qrcode

FusionCharts.
DSpace Software Coptright(c) 2010 MIT and Hewleft-Packard  /  KRIBB-REPOSITORY ( Email:jakim@kribb.re.kr)