TERNARY COMPLEX OF AN ACTIVE SITE DOUBLE MUTANT OF HORSE LIVER ALCOHOL DEHYDROGENASE, PHE93=>TRP, VAL203=>ALA WITH NAD AND TRIFLUOROETHANOL

Active site modifications in a double mutant of liver alcohol dehydrogenase: structural studies of two enzyme-ligand complexes.

A Link between Protein Structure and Enzyme Catalyzed Hydrogen Tunneling

4MICROLITER HANGING DROPS TRIS PH 8.4 AT 4C, 5MM TRIFLUROETHANOL, 4% PEG400 EQUILIBRATED AGAINST WELLS CONTAINING 5MM TFE AND 18%PEG 400, vapor diffusion - hanging drop

UP TO LAST CG MINIMIZATION THROUGHOUT UNTIL LAST CG REFINEMENT

OXIDOREDUCTASE (NAD(A)-CHOH(D)), LIVER, ALCOHOL, DEHYDROGENASE, LADH, ACTIVE SITE MUTANT, OXIDOREDUCTASE