Crystallization and purification of the enzyme anthranilate phosphoribosyl transferase.
Anthranilate phosphoribosyl transferase from the bacterium Hafnia alvei has been crystallized. This enzyme is one of a small number that constitute the biosynthetic pathway for tryptophan. Large cubic crystals were grown at 4 degrees C by dialyzing away the glycerol from a protein solution that included ammonium sulfate, polyethylene glycol and glycerol. The crystals were much more temperature stable and resistant to X-ray deterioration than a previous, similar crystal form that had included glycerol. The crystals belong to the space group I432, a = b = c = 189 A (1 A = 0.1 nm). The ratio of the monomer molecular weight, 37,000, to the volume of the unit cell suggests that there is one homodimer per asymmetric unit. The crystals diffracted to a resolution of 3.0 A at the Stanford Synchotron Radiation Laboratory X-ray source.
Edwards
S L
SL
Department of Chemistry, University of California, San Diego, La Jolla 92093.
Kraut
J
J
Xuong
N
N
Ashford
V
V
Halloran
T P
TP
Mills
S E
SE
D000877:Anthranilate Phosphoribosyltransferase; D003460:Crystallization; D004755:Enterobacteriaceae / Q000201:enzymology*; D010430:Pentosyltransferases; D014961:X-Ray Diffraction
D010430:Pentosyltransferases; D000877:Anthranilate Phosphoribosyltransferase