Crystal structure of Putative phosphoribosylformylglycinamidine cyclo-ligase (YP_676759.1) from CYTOPHAGA HUTCHINSONII ATCC 33406 at 1.50 A resolution

Joint Center for Structural Genomics (JCSG)

Single crystal Si(111) bent monochromator (horizontal focusing)

Phosphoribosylformylglycinamidine cyclo-ligase

0.2000M KAcetate, 20.0000% PEG-3350, No Buffer pH 7.8, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K

THIS CONSTRUCT 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.ATOM RECORDS CONTAIN RESIDUAL B FACTORS ONLY. 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 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 4.ACETATE (ACT) AND 1,2-ETHANEDIOL (EDO) FROM THE CRYSTALLIZATION AND CRYOPROTECTANT SOLUTION HAVE BEEN MODELED IN THE SOLVENT STRUCTURE.

ANALYTICAL SIZE-EXCLUSION CHROMATOGRAPHY SUPPORTS THE ASSIGNMENT OF A DIMER AS THE SIGNIFICANT OLIGOMERIC FORM IN SOLUTION.

Putative phosphoribosylformylglycinamidine cyclo-ligase, Structural Genomics, Joint Center for Structural Genomics, JCSG, Protein Structure Initiative, PSI-2, Ligase