Authors state that the biologically relevant molecule is generated by applying the crystallographic symmetry operations X-Y, -Y, 1/3-Z to the first half of the protein.
-
Components
#1: Protein
TANDEMCYANOVIRIN-NDIMERCVN2L0 / CV-N
Mass: 23368.639 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Nostoc ellipsosporum (bacteria) / Plasmid: pET11a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P81180
Resolution: 2→23.93 Å / Cor.coef. Fo:Fc: 0.945 / Cor.coef. Fo:Fc free: 0.931 / WRfactor Rfree: 0.2484 / WRfactor Rwork: 0.2153 / Occupancy max: 1 / Occupancy min: 0 / FOM work R set: 0.7758 / SU B: 5.81 / SU ML: 0.156 / SU R Cruickshank DPI: 0.2171 / SU Rfree: 0.1765 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.176 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: (1) Only half of the crystallized molecule is in the asymmetric unit. The entire polypeptide chain (biologically relevant molecule) is generated by the operations: X-Y, -Y, 1/3-Z. (2) ...Details: (1) Only half of the crystallized molecule is in the asymmetric unit. The entire polypeptide chain (biologically relevant molecule) is generated by the operations: X-Y, -Y, 1/3-Z. (2) HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.2488
341
4.6 %
RANDOM
Rwork
0.2196
-
-
-
all
0.221
7710
-
-
obs
0.221
7369
99.17 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
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