wwPDB validation report of PDB entry 3H41

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 24-333 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. RAMACHANDRAN OUTLIER PRO305 IS SUPPORTED BY DENSITY. 4. CYS238 IS OXIDIZED AS CYSTEINE SULFONIC ACID (OCS). 5. THE ALA-D-GAMMA-GLU MODELED IN THE ACTIVE SITE IS BASED ON DENSITY AND FUNCTION OF THE PROTEIN. PHOSPHATE AND PEG FRAGEMENTS ARE PRESENTS IN CRYSTALLIZATION CONDITIONS.

CRYSTAL STRUCTURE OF A NLPC/P60 FAMILY PROTEIN (BCE_2878) FROM BACILLUS CEREUS ATCC 10987 AT 1.79 A RESOLUTION

The largest off-origin peak in the Patterson function is 6.59% 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)