Crystal structure of acetoin utilization protein (ZP_00540088.1) from Exiguobacterium sibiricum 255-15 at 2.33 A resolution

Joint Center for Structural Genomics (JCSG)

Flat collimating mirror, toroid focusing mirror

NANODROP, 5.7% PEG 8000, 0.2M Calcium acetate, 0.1M Imidazole pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K

BIOMOLECULE: 1, 2, 3, 4, 5, 6
THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
WHICH CONSISTS OF 6 CHAIN(S). SEE REMARK 350 FOR
INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
SIZE EXCLUSION CHROMATOGRAPHY WITH STATIC LIGHT SCATTERING
SUPPORT THE ASSIGNMENT OF A MONOMER AS A BIOLOGICALLY
SIGNIFICANT OLIGOMERIZATION STATE.

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 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 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET
INCORPORATION.
4. CALCIUM AND ACETATE FROM THE CRYSTALLIZATION SOLUTIONS WERE
MODELED INTO THE STRUCTURE.
5. ETHYLENE GLYCOL USED AS A CRYOPROTECTANT WAS MODELED INTO THE
STRUCTURE.
6. UNEXPLAINED DIFFERENCE ELECTRON DENSITIES NEAR GLY 112 IN
THE D AND E SUBUNITS WERE NOT MODELED.
7. ARG B205, PHE B207, ASP C35, AND PRO C36 WERE MODELED INTO
ELECTRON DENSITY BUT ARE RAMACHANDRAN OUTLIERS.

SIZE EXCLUSION WITH STATIC LIGHT SCATTERING SUPPORTS THE ASSIGNMENT OF A MONOMER AS A BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE.

ZP_00540088.1, acetoin utilization protein, Structural Genomics, Joint Center for Structural Genomics, JCSG, Protein Structure Initiative, PSI-2, TRANSFERASE