H: HUMAN FAB ANTIBODY FRAGMENT OF CBTAU-28.1(S32R;E35K) L: HUMAN FAB ANTIBODY FRAGMENT OF CBTAU-28.1(S32R;E35K) I: TAU PEPTIDE A7731 (RESIDUES 52-71) hetero molecules
Mass: 23992.936 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human)
#2: Antibody
HUMANFABANTIBODYFRAGMENTOFCBTAU-28.1(S32R;E35K)
Mass: 24312.900 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
TAUPEPTIDEA7731 (RESIDUES52-71)
Mass: 2025.963 Da / Num. of mol.: 1 / Fragment: FAB ANTIBODY FRAGMENT / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: P10636*PLUS
Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Oct 28, 2016
Radiation
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 0.9999 Å / Relative weight: 1
Reflection
Resolution: 2.85→70.95 Å / Num. obs: 11082 / % possible obs: 99.1 % / Observed criterion σ(I): 0 / Redundancy: 3.8 % / Rmerge(I) obs: 0.112 / Net I/σ(I): 10.52
Reflection shell
Resolution: 2.85→3.1 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0.447 / % possible all: 98.1
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Processing
Software
Name
Version
Classification
XDS
datareduction
XSCALE
datascaling
REFMAC
5.8.0049
refinement
PHASER
phasing
Refinement
Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.85→70.95 Å / Cor.coef. Fo:Fc: 0.907 / Cor.coef. Fo:Fc free: 0.86 / SU B: 21.56 / SU ML: 0.389 / Cross valid method: THROUGHOUT / ESU R Free: 0.473 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.27814
683
6.2 %
RANDOM
Rwork
0.23592
-
-
-
obs
0.23854
10362
98.99 %
-
Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å