Literature summary for 6.3.4.14 extracted from

Kondo, S.; Nakajima, Y.; Sugio, S.; Sueda, S.; Islam, M.N.; Kondo, H.
Structure of the biotin carboxylase domain of pyruvate carboxylase from Bacillus thermodenitrificans (2007), Acta Crystallogr. Sect. D, 63, 885-890.

Crystallization (Commentary)

Crystallization (Comment)	Organism
the biotin carboxylase domain of pyruvate carboxylase from Bacillus thermodenitrificans is crystallized in an orthorhombic form (space group P2(1)2(1)2(1)), with unit-cell parameters a = 79.6 A, b = 116.0 A, c = 115.7 A by hanging-drop vapour-diffusion method. Two biotin carboxylase protomers are contained in the asymmetric unit. Diffraction data are collected at -173°C and the crystal structure is solved by the molecular-replacement method and refined against reflections in the 20.02.4 A resolution range	Geobacillus thermodenitrificans

Crystallization (Comment)

Organism

the biotin carboxylase domain of pyruvate carboxylase from Bacillus thermodenitrificans is crystallized in an orthorhombic form (space group P2(1)2(1)2(1)), with unit-cell parameters a = 79.6 A, b = 116.0 A, c = 115.7 A by hanging-drop vapour-diffusion method. Two biotin carboxylase protomers are contained in the asymmetric unit. Diffraction data are collected at -173°C and the crystal structure is solved by the molecular-replacement method and refined against reflections in the 20.02.4 A resolution range

Geobacillus thermodenitrificans

Organism

Organism	UniProt	Comment	Textmining
Geobacillus thermodenitrificans	-	-	-

Subunits

Subunits	Comment	Organism
dimer	-	Geobacillus thermodenitrificans

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Release 2023.1 (January 2023)