Crystal structure of an auxiliary nutrient binding protein (BT_3476) from Bacteroides thetaiotaomicron VPI-5482 at 2.23 A resolution

Joint Center for Structural Genomics (JCSG)

Crystal structure of a Hypothetical hydrolase (BT_3476) from Bacteroides thetaiotaomicron VPI-5482 at 2.23 A resolution

20.00% polyethylene glycol 3350, 0.20M sodium dihydrogen phosphate, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K

THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY RESIDUES 29-457 OF THE TARGET SEQUENCE.

1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS 2. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. 3. 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 TO ACCOUNT FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 4. 1,2 ETHANEDIOL (EDO) AND PHOSPATE (PO4) FROM THE CRYSTALLIZATION CONDITIONS AND CHLORIDE (CL)FROM THE EXPRESSION OR PURIFICATION BUFFERS HAVE BEEN MODELED IN THE SOLVENT STRUCTURE. 5. NCS RESTRAINTS WERE APPLIED USING BUSTER'S LSSR RESTRAINT REPRESENTATION (-AUTONCS). 6. THE REFINEMENT WAS RESTRAINED AGAINST THE MAD PHASES.

6-bladed beta-propeller, Immunoglobulin-like, Structural Genomics, Joint Center for Structural Genomics, JCSG, Protein Structure Initiative, PSI-BIOLOGY, HYDROLASE