wwPDB validation report of PDB entry 3EU8

Flat collimating mirror, toroid focusing mirror

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 23-451 OF THE FULL LENGTH PROTEIN.

1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
2. 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.
3. ATOM RECORDS CONTAIN RESIDUAL B FACTORS ONLY.
4. POTASSIUM, ETHYLENE GLYCOL AND CHLORIDE,
PRESENT IN CRYSTALLIZATION/CRYO CONDITIONS, WERE
MODELED INTO THE STRUCTURE.
5. THE CIS PEPTIDES BETWEEN 222-223 ARE SUPPORTED BY
WELL DEFINED DENSITY.

Crystal structure of putative glucoamylase (YP_210071.1) from Bacteroides fragilis NCTC 9343 at 2.12 A resolution

The largest off-origin peak in the Patterson function is 3.29% 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)