Preliminary X-ray crystallographic analysis of tryptophanase from Escherichia coli.
Tryptophanase (L-tryptophan indole-lyase) from Escherichia coli has been crystallized from ammonium sulfate solution using a vapor diffusion method. The crystals are tetragonal and belong to space group P4(1)2(1)2 or its enantiomorph. The cell dimensions of the crystals are a = b = 113.4 A, and c = 232.2 A, with two subunits per asymmetric unit. The crystals diffract to at least 3 A resolution, and are suitable for X-ray structural analysis.
Kawata
Y
Y
Department of Chemistry, Faculty of Science, Kyoto University, Japan.
Tani
S
S
Sato
M
M
Katsube
Y
Y
Tokushige
M
M
D000645:Ammonium Sulfate; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003460:Crystallization; D004926:Escherichia coli / Q000201:enzymology*; D012996:Solutions; D014368:Tryptophanase / Q000737:chemistry*; D014961:X-Ray Diffraction
D012996:Solutions; D014368:Tryptophanase; D000645:Ammonium Sulfate