Crystal structure of putative cystathionine beta-lyase involved in aluminum resistance (NP_348457.1) from Clostridium acetobutylicum at 2.00 A resolution

Joint Center for Structural Genomics (JCSG)

(2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid

Flat collimating mirror, toroid focusing mirror

Cystathionine beta-lyase family protein, YNBB B.subtilis ortholog

DATA WERE SCALED USING XSCALE WITH FRIEDEL PAIRS KEPT AS SEPARATE WHEN COMPUTING R-SYM, COMPLETENESS AND <I/SIGMA(I)>.

0.9500M sodium citrate, 0.1M sodium cacodylate pH 6.43, 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 THE TARGET SEQUENCE.

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. SODIUM (NA) CATIONS AND ETHYLENE GLYCOL (EDO) MOLECULES FROM CRYSTALLIZATION AND CRYOPROTECTION SOLUTIONS WERE MODELED INTO THE STRUCTURE

ANALYTICAL SIZE EXCLUSION CHROMATOGRAPHY WITH STATIC LIGHT SCATTERING SUPPORTS THE ASSIGNMENT OF A TETRAMER AS A SIGNIFICANT OLIGOMERIZATION STATE IN SOLUTION.

NP_348457.1, PUTATIVE CYSTATHIONINE BETA-LYASE INVOLVED IN ALUMINUM RESISTANCE, Structural Genomics, Joint Center for Structural Genomics, JCSG, Protein Structure Initiative, PSI-2, Lyase, Aluminium resistance protein