Literature summary for 3.5.3.11 extracted from

Lee, J.A.; Ahn, H.J.; Ha, J.Y.; Shim, S.M.; Kim, K.H.; Kim, H.K.; Suh, S.W.
Crystallization and preliminary X-ray crystallographic analysis of a putative agmatinase from Deinococcus radiodurans (2004), Acta Crystallogr. Sect. D, 60, 1890-1892.

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli as a fusion protein with the C-terminal eight-residue His-tag	Deinococcus radiodurans

Crystallization (Commentary)

Crystallization (Comment)	Organism
hangimg-drop vapor-diffusion method, crystallized at 297 K using polyethylene glycol 3000 as a precipitant. X-ray diffraction data are collected to 1.8 A from a crystal grown in the presence of Mn2+ and 1,6-hexanediamine. The crystals are orthorhombic, belonging to the space group P2(1)2(1)2(1), with unit-cell parameters a = 81.77 A, b = 131.44 A, c = 168.85 A, alpha = beta = gamma = 90°. A hexameric molecule is likely to be present in the asymmetric unit	Deinococcus radiodurans

Crystallization (Comment)

Organism

hangimg-drop vapor-diffusion method, crystallized at 297 K using polyethylene glycol 3000 as a precipitant. X-ray diffraction data are collected to 1.8 A from a crystal grown in the presence of Mn2+ and 1,6-hexanediamine. The crystals are orthorhombic, belonging to the space group P2(1)2(1)2(1), with unit-cell parameters a = 81.77 A, b = 131.44 A, c = 168.85 A, alpha = beta = gamma = 90°. A hexameric molecule is likely to be present in the asymmetric unit

Deinococcus radiodurans

Organism

Organism	UniProt	Comment	Textmining
Deinococcus radiodurans	-	-	-

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Release 2023.1 (January 2023)