Literature summary for 4.2.1.20 extracted from

Jeong, M.S.; Jang, S.B.
Crystallization and X-ray crystallographic studies of wild-type and mutant tryptophan synthase alpha-subunits from Escherichia coli (2005), Mol. Cells, 19, 219-222.

Cloned(Commentary)

Cloned (Comment)	Organism
wild-type and P28L/Y173F double mutant alpha-subunits are overexpressed in Escherichia coli	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
wild-type and P28L/Y173F double mutant alpha-subunits are crystallized at 25°C by the hanging-drop vapor-diffusion method. X-ray diffraction data are collected to 2.5 A resolution from the wild-type crystals and to 1.8 A from the crystals of the double mutant. The wild-type crystals belonged to the monoclinic space group C2 (a = 155.64 A, b = 44.54 A, c = 71.53 A and beta = 96.39°) and the P28L/Y173F crystals to the monoclinic space group P 2(1) (a = 71.09 A, b = 52.70 A, c = 71.52 A, and beta = 91.49°). The asymmetric unit of both structures contains two molecules of tryptophan synthase alpha-subunit	Escherichia coli

Crystallization (Comment)

Organism

wild-type and P28L/Y173F double mutant alpha-subunits are crystallized at 25°C by the hanging-drop vapor-diffusion method. X-ray diffraction data are collected to 2.5 A resolution from the wild-type crystals and to 1.8 A from the crystals of the double mutant. The wild-type crystals belonged to the monoclinic space group C2 (a = 155.64 A, b = 44.54 A, c = 71.53 A and beta = 96.39°) and the P28L/Y173F crystals to the monoclinic space group P 2(1) (a = 71.09 A, b = 52.70 A, c = 71.52 A, and beta = 91.49°). The asymmetric unit of both structures contains two molecules of tryptophan synthase alpha-subunit

Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
P28L/Y173F	wild-type crystals belonged to the monoclinic space group C2 (a = 155.64 A, b = 44.54 A, c =71.53 A and beta = 96.39°) and the P28L/Y173F crystals to the monoclinic space group P 2(1) (a = 71.09 A, b = 52.70 A, c = 71.52 A, and beta = 91.49°). The asymmetric unit of both structures contains two molecules of tryptophan synthase alpha-subunit	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

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Release 2023.1 (January 2023)