Crystal structure of a nifx-associated protein of unknown function (afe_1514) from acidithiobacillus ferrooxidans atcc at 2.00 A resolution
Joint Center for Structural Genomics (JCSG)
Crystal structure of NifX-associated protein of unknown function (YP_002425942.1) from Acidithiobacillus ferrooxidans ATCC 23270 at 2.00 A resolution
Flat collimating mirror, toroid focusing mirror
G(MSE)PENTA(MSE)AALLPEESLFFRELVKQWRAQDSYGTWEKKSD(MSE)ELLAPYVLDKEQRRAIPIIGDPDPEIL WRVELFYNAVGLATERASGV(MSE)VSP(MSE)(MSE)K(MSE)SHEGFGR(MSE)VLIAGRLIVVNKQLRDVHRFGFPS (MSE)EKLAEEGDKLVAGALE(MSE)IEKFPEVARF
GMPENTAMAALLPEESLFFRELVKQWRAQDSYGTWEKKSDMELLAPYVLDKEQRRAIPIIGDPDPEILWRVELFYNAVGL ATERASGVMVSPMMKMSHEGFGRMVLIAGRLIVVNKQLRDVHRFGFPSMEKLAEEGDKLVAGALEMIEKFPEVARF
Acidithiobacillus ferrooxidans ATCC 23270
NANODROP, 0.20M Li2SO4, 30.0% PEG 4000, 0.1M Tris-HCl pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K
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. THE CLONED CONSTRUCT CONTAINS RESIDUES 22-363 OF THE FULL LENGTH PROTEIN.
1. HYDROGENS HAVE BEEN ADDED IN THE 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), A CRYOPROTECTANT WAS MODELED INTO THE STRUCTURE. 5. SULFATE MOLECULES (SO4), AND POLYETHYLENE GLYCOL (PG6) FROM THE CRYSTALLIZATION SOLUTION WERE MODELED INTO THE STRUCTURE.
Duf 269 family protein, structural genomics, Joint Center for Structural Genomics, JCSG, Protein Structure Initiative, PSI-2, unknown function
MPENTAMAALLPEESLFFRELVKQWRAQDSYGTWEKKSDMELLAPYVLDKEQRRAIPIIGDPDPEILWRVELFYNAVGLA TERASGVMVSPMMKMSHEGFGRMVLIAGRLIVVNKQLRDVHRFGFPSMEKLAEEGDKLVAGALEMIEKFPEVARF