Crystal structure of a Putative thua-like protein (BACUNI_01602) from Bacteroides uniformis ATCC 8492 at 1.50 A resolution

Joint Center for Structural Genomics (JCSG)

Crystal structure of a hypothetical protein (BACUNI_01602) from Bacteroides uniformis ATCC 8492 at 1.50 A resolution

Flat mirror (vertical focusing); single crystal Si(111) bent monochromator (horizontal focusing)

0.1M MES pH 6, 10% polyethylene glycol 8000, 0.2M zinc acetate, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 293K

SEQUENCE THIS CONSTRUCT (RESIDUES 19-267) 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. 2-(N-MORPHOLINO)-ETHANESULFONIC ACID (MES), ZINC (ZN), AND 1,2-ETHANEDIOL (EDO) FROM THE CRYSTALLIZATION/CRYO CONDITIONS, AND CHLORIDE (CL) AND SODIUM FROM THE PURIFICATION BUFFERS HAVE BEEN MODELED INTO THE STRUCTURE.4.ATOM RECORDS CONTAIN SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. 5.WATERS WERE EXCLUDED FROM AUTOMATIC TLS ASSIGNMENT 6. REFINEMENTS WERE PERFORMED USING THE SAD TARGET FUNCTION OF REFMAC TO ESTIMATE THE OCCUPANCIES OF THE ZN SITES.

Trehalose utilization, PF06283 family protein, Structural Genomics, Joint Center for Structural Genomics, JCSG, Protein Structure Initiative, PSI-BIOLOGY, UNKNOWN FUNCTION