Crystal structure of a putative dipeptidyl-peptidase VI (BACOVA_00612) from Bacteroides ovatus at 1.72 A resolution

Joint Center for Structural Genomics (JCSG)

Flat collimating mirror, toroid focusing mirror

15.000000000% Glycerol, 0.170000000M NaOAc, 25.500000000% PEG-4000, 0.1M TRIS pH 8.5, NANODROP', VAPOR DIFFUSION, SITTING DROP, temperature 277K

THE CONSTRUCT (RESIDUES 22-326) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.

1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 3. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. 4. WATERS WERE EXCLUDED FROM AUTOMATIC TLS ASSIGNMENT. 5. GLYCEROL (GOL) AND CHLORIDE (CL) MODELED ARE PRESENT IN CRYSTALLIZATION/CRYO CONDITIONS. 6. ACTIVE SITE RESIDUE CYS203 IS COVALENTLY MODIFIED. IT IS MODELED AS S-ACETONYLCYSTEINE (CSA) BASED ON DENSITY AND INTERACTION ENVIROMENT.

Structural Genomics, Joint Center for Structural Genomics, JCSG, Protein Structure Initiative, PSI-2, HYDROLASE