L: HUMAN FAB ANTIBODY FRAGMENT OF CBTAU-27.1(S31Y,T100I) H: HUMAN FAB ANTIBODY FRAGMENT OF CBTAU-27.1(S31Y,T100I) A: HUMAN TAU PEPTIDE A8119 RESIDUES 299-318 hetero molecules
Mass: 24116.666 Da / Num. of mol.: 1 / Fragment: FAB ANTIBODY FRAGMENT Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human)
#2: Antibody
HUMANFABANTIBODYFRAGMENTOFCBTAU-27.1(S31Y,T100I)
Mass: 23952.826 Da / Num. of mol.: 1 / Fragment: FAB ANTIBODY FRAGMENT Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human)
#3: Protein/peptide
HUMANTAUPEPTIDEA8119RESIDUES299-318
Mass: 1262.537 Da / Num. of mol.: 1 / Fragment: FAB ANTIBODY FRAGMENT / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: P10636*PLUS
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 1 Å / Relative weight: 1
Reflection
Resolution: 2.95→88.2 Å / Num. obs: 10377 / % possible obs: 98 % / Observed criterion σ(I): 0 / Redundancy: 2.8 % / Rmerge(I) obs: 0.128 / Net I/σ(I): 9.5
Reflection shell
Resolution: 2.95→3.2 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.457 / % possible all: 98.9
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Processing
Software
Name
Version
Classification
XDS
datareduction
XSCALE
datascaling
REFMAC
5.8.0151
refinement
Refinement
Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.95→88.2 Å / Cor.coef. Fo:Fc: 0.906 / Cor.coef. Fo:Fc free: 0.86 / SU B: 0.465 / SU ML: 0.405 / Cross valid method: THROUGHOUT / ESU R Free: 0.481 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.26778
643
6.2 %
RANDOM
Rwork
0.22049
-
-
-
obs
0.22352
9734
98.04 %
-
Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å