Crystal structure of E. coli glyoxylate carboligase

Glyoxylate carboligase lacks the canonical active site glutamate of thiamine-dependent enzymes.

2-4 microlitre of protein solution (5-15 mg/ml, 100 micromolar ThDP, 10 micromolar FAD, 1mM MgCl2 and 10 mM quinone Q0) were mixed with equal volume of reservoir solution (0.5% PEG6000, 0.5M NaCl, 40 mM DTT), pH 8.00, VAPOR DIFFUSION, HANGING DROP, temperature 294.K

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
The asymmetric contains 6 monomers. Four monomers (chains C,D,E,F) form one complete tetramer. Two monomers (chains A,B) form tetramer by rotation around the diagonal 2-fold in the ab plane at z=1/4 (symmop 8 of the spacegroup: -y,-x,-z+1/2), followed by 0,0,-1 translation
thiamin-diphosphate (ThDP), thimain-dependent enzymes, FAD, enzyme, glyoxylate carboligase, Lyase