Crystallization and preliminary structural studies of a chorismate mutase catalytic antibody complexed with a transition state analog.
The Fab' fragment of a catalytic antibody with chorismate mutase activity has been crystallized as a complex with the transition-state analog hapten. The complex was crystallized by the vapor diffusion method using ammonium sulfate as the precipitant. The crystals belong to the orthorhombic space group P2(1)2(1)2(1) with unit cell dimensions a = 37.1 A, b = 63.3 A, c = 178.5 A, and there is one Fab' molecule per asymmetric unit. The crystals diffract X-rays to at least 3.0 A and are suitable for X-ray crystallographic studies.
Haynes
M R
MR
Department of Molecular Biology, Scripps Research Institute, La Jolla, California 92037.
Stura
E A
EA
Hilvert
D
D
Wilson
I A
IA
D000818:Animals; D017151:Antibodies, Catalytic / Q000737:chemistry*; D000911:Antibodies, Monoclonal / Q000737:chemistry; D002826:Chorismate Mutase / Q000737:chemistry* / Q000276:immunology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D006241:Haptens / Q000737:chemistry; D007140:Immunoglobulin Fab Fragments / Q000737:chemistry; D051379:Mice
D017151:Antibodies, Catalytic; D000911:Antibodies, Monoclonal; D006241:Haptens; D007140:Immunoglobulin Fab Fragments; D002826:Chorismate Mutase