wwPDB validation report of PDB entry 3GUX

Single crystal Si(111) bent monochromator (horizontal focusing)

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 22-334 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.ACETATE ION AND ETHYLENE GLYCOL MOLECULE FROM CRYSTALLIZATION AND CROPROTECTION CONDITIONS ARE MODELED IN THE STRUCTURE. 5.A RAMACHANDRAN OUTLIER IS OBSERVED ON RESIDUE 196 OF CHAIN A IN A REGION OF POOR ELECTRON DENSITY.

Crystal structure of a putative zn-dependent exopeptidase (bvu_1317) from bacteroides vulgatus atcc 8482 at 1.80 A resolution

THE RESULTS FROM SIZE EXCLUSION CHROMATOGRAPHY SUPPORTS THE ASSIGNMENT OF A MONOMER AS A SIGNIFICANT OLIGOMERIZATION STATE.

The largest off-origin peak in the Patterson function is 4.62% of the height of the origin peak. No significant pseudotranslation is detected.

structure factor analysis and validation

geometric validation package for ligand chemistry in protein x-ray structures

20191225.v01 (using entries in the PDB archive December 25th 2019)