Crystallization and initial crystallographic characterization of the Corynebacterium glutamicum nitrilotriacetate monooxygenase component A.
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 A 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 A, beta = 101.94 degrees . The asymmetric unit consists of four molecules, corresponding to a packing density of 2.3 A(3) Da(-1). The structure was solved by molecular replacement. Structure refinement is in progress.
Kim
Kyung-Jin
KJ
Beamline Division, Pohang Accelerator Laboratory, Pohang, Kyungbuk 790-784, South Korea. kkj@postech.ac.kr
Kim
Sujin
S
Lee
Sujin
S
Kang
Beom Sik
BS
Lee
Heung-Soo
HS
Oh
Tae-Kwang
TK
Kim
Myung Hee
MH
D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification; D002850:Chromatography, Gel; D003352:Corynebacterium / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D007700:Kinetics; D006899:Mixed Function Oxygenases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D008970:Molecular Weight; D021122:Protein Subunits / Q000737:chemistry / Q000302:isolation & purification
D001426:Bacterial Proteins; D021122:Protein Subunits; D006899:Mixed Function Oxygenases; C072680:nitrilotriacetate monooxygenase