Literature summary for 2.4.1.B64 extracted from

Martinez-Fleites, C.; Proctor, M.; Roberts, S.; Bolam, D.N.; Gilbert, H.J.; Davies, G.J.
Insights into the synthesis of lipopolysaccharide and antibiotics through the structures of two retaining glycosyltransferases from family GT4 (2006), Chem. Biol., 13, 1143-1152.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
crystals of the enzyme and of its selenomethionine derivative are grown in 0.1 M MES (pH 6.75), 0.2 M NaBr, and 15% PEG 3350 at a protein concentration of 10 mg/ml. Microseeding is necessary to achieve reproducibility of the crystals. Crystals of the complex of the enzyme with UDP-2F-glucose are prepared by addition of 10 mM UDP-2F-glucose to the protein solution prior to crystallization. The structure of the enzyme is solved by single-wavelength anomalous dispersion with a selenomethionine version of the protein, at a resolution of 1.6 A, in the presence of UDP	Escherichia coli

Crystallization (Comment)

Organism

crystals of the enzyme and of its selenomethionine derivative are grown in 0.1 M MES (pH 6.75), 0.2 M NaBr, and 15% PEG 3350 at a protein concentration of 10 mg/ml. Microseeding is necessary to achieve reproducibility of the crystals. Crystals of the complex of the enzyme with UDP-2F-glucose are prepared by addition of 10 mM UDP-2F-glucose to the protein solution prior to crystallization. The structure of the enzyme is solved by single-wavelength anomalous dispersion with a selenomethionine version of the protein, at a resolution of 1.6 A, in the presence of UDP

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P25740	-	-

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Release 2023.1 (January 2023)