Crystal structure of a putative outer membrane chaperone (OmpH-like) (CC_1914) from Caulobacter crescentus CB15 at 2.83 A resolution (PSI Community Target, Shapiro)
Joint Center for Structural Genomics (JCSG)
Flat mirror (vertical focusing); single crystal Si(111) bent monochromator (horizontal focusing)
Putative outer membrane chaperone (OmpH-like)
(MSE)GSDKIHHHHHHENLYFQGTHGPALPGVCIFSSPRAVGSSLVGKAVDARLKTIIQQVNAELTGERTALDNEAKALD AKKTTIAQDALEQQAATLQAKANAWQRKGQLRQKEVEATEQKALSRVYQELNTPIQQVYQAQKCSVLLDREAV(MSE)LA NPA(MSE)DITDAVVAALDARIKTLTFDRERLDQQVPGAAALQPTNK
MGSDKIHHHHHHENLYFQGTHGPALPGVCIFSSPRAVGSSLVGKAVDARLKTIIQQVNAELTGERTALDNEAKALDAKKT TIAQDALEQQAATLQAKANAWQRKGQLRQKEVEATEQKALSRVYQELNTPIQQVYQAQKCSVLLDREAVMLANPAMDITD AVVAALDARIKTLTFDRERLDQQVPGAAALQPTNK
0.20M sodium chloride, 40.00% polyethylene glycol 400, 0.1M Na/K phosphate pH 6.2, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 293K
THE CONSTRUCT (37-212) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG.
1. 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. 2. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. 3. THE MAD PHASES WERE USED AS RESTRAINTS DURING REFINEMENT. 4. PEG MODELED IS PRESENT IN CRYO/CRYSTALLIZATION CONDITIONS. 5. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 6. ZERO-OCCUPANCY ATOMS WERE PLACED NEAR THE THREE-FOLD AXIS TO EXCLUDE SOLVENT MASK NEAR THIS REGION. 7. WATERS WERE EXCLUDED FROM AUTOMATIC TLS ASSIGNMENT.
PF03938 family, Structural Genomics, Joint Center for Structural Genomics, JCSG, Protein Structure Initiative, PSI-BIOLOGY, CHAPERONE
THGPALPGVCIFSSPRAVGSSLVGKAVDARLKTIIQQVNAELTGERTALDNEAKALDAKKTTIAQDALEQQAATLQAKAN AWQRKGQLRQKEVEATEQKALSRVYQELNTPIQQVYQAQKCSVLLDREAVMLANPAMDITDAVVAALDARIKTLTFDRER LDQQVPGAAALQPTNK