Crystal structure of a putative dna binding protein (ape_0880a) from aeropyrum pernix k1 at 2.21 A resolution
Joint Center for Structural Genomics (JCSG)
Crystal structure of uncharacterized protein (NP_147569.1) from Aeropyrum pernix at 2.21 A resolution
Flat collimating mirror, toroid focusing mirror
G(MSE)DDETLRLQFGHLIRILPTLLEFEKKGYEPSLAEIVKASGVSEKTFF(MSE)GLKDRLIRAGLVKEETLSYRVKT LKLTEKGRRLAECLEKCRDVLGS
GMDDETLRLQFGHLIRILPTLLEFEKKGYEPSLAEIVKASGVSEKTFFMGLKDRLIRAGLVKEETLSYRVKTLKLTEKGR RLAECLEKCRDVLGS
NANODROP, 1.0M LiCl, 10.0% PEG 6000, 0.1M Citrate pH 4.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K
SEQUENCE THE 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 RIDING POSITIONS. 2. ATOM RECORD CONTAINS 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 TO ACCOUNT FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 4. ETHYLENE GLYCOL (EDO) FROM THE CRYOPROTECTANT, CITRATE (CIT) AND CL IONS FROM THE CRYSTALLIZATION BUFFER WERE MODELED INTO THE STRUCTURE. 5. PEG6000 FRAGMENTS (PEG) FROM CRYSTALLIZATION SOLUTION ARE MODELLED. 6. THE SIDE CHAIN OF THE RESIDUE 48 IN THE A SUBUNIT WAS DISORDERED AND WAS NOT MODELED.
Structural genomics, Joint Center for Structural Genomics, JCSG, Protein Structure Initiative, PSI-2, dna binding protein
MDDETLRLQFGHLIRILPTLLEFEKKGYEPSLAEIVKASGVSEKTFFMGLKDRLIRAGLVKEETLSYRVKTLKLTEKGRR LAECLEKCRDVLGS