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. 2018 Nov 13;7:e38922. doi: 10.7554/eLife.38922

Table 3. X-ray Crystallographic and Refinement statistics of MT polymerase:αβ-tubulin:DRP.

Data collection 1:2:2 sk-Alp14-monomer:
αβ-Tubulin:DRP
1:2:2 sk-Alp14-monomer-SL:
αβ-Tubulin:DRP
1:2:2 sk-Alp14-monomer:
αβ-Tubulin:DRPΔN
1:2:2 sk-Alp14-dimer:
αβ-Tubulin:DRPΔN
Resolution range (Å) 96.59 - 4.40 (4.64- 4.40)* 59.45 – 3.60 (3.79 – 3.60)* 57.56 – 3.20 (3.37 – 3.20)* 99.83 – 3.5 (3.69 – 3.50)*
Space group P 21 P 21 P 21 P 21
Wavelength (Å) 0.9792 0.9792 0.9792 0.9792
Unit cell (Å): a, b, c
(°): β
218.80, 107.65, 282.74
90.38
218.48, 106.15, 282.23
90.39
115.13, 194.99, 149.57
90.19
122.73 199.67, 162.70
90.09
Total number of observed reflections 229567 380856 298551 235576
Unique reflections 80099 {68039} 142673 {121943} 104265 {88337} 91368
Average mosaicity 0.57 0.38 0.64 0.50
Multiplicity 2.9 (2.9)* 2.7 (2.7)* 2.9 (2.9)* 2.6 (2.4)*
Completeness (%) 95.4 (94.8) {80.6} 95.0 (96.7) {79.0} 96.2 (97.9) {82.0} 92.9 (90.2)*
Wilson B-factor (Å2) 82.7 81.4 46.6 -
<I/σ (I)> 4.9 (1.9)* 4.8 (1.2)* 5.8 (1.5)* 4.8 (1.1)*
Rmergec 0.14 (0.48)* 0.13(0.65)* 0.13(0.65)* 0.14 (0.63)*
Structure refinement
Rwork 0.23 (0.26)* 0.20 (0.24)* 0.18 (0.23)* -
Rfree 0.26 (0.33)* 0.24 (0.26)* 0.24 (0.26)* -
Complexes per asymmetric unit 2 2 2 -
Number of atoms 78030 77878 36865 -
Protein residues 9989 9981 4661 -
Ligand atoms 496 496 248 -
RMS bond lengths (Å) 0.004 0.004 0.004 -
RMS bond angles (°) 0.94 0.98 0.93 -
Ramachandran favored (%) 94.0 94.0 95.0 -
Ramachandran allowed (%) 5.4 5.5 4.5
Ramachandran outliers (%) 0.3 0.3 0.2 -
Clashscore 4.5 4.8 5.6 -
Mean B values (Å2)
Overall 108.4 98.3 48.6 -
Macromolecules 108.6 98.4 48.6 -
Ligands 78.5 91.5 36.4 -

*Numbers represent the highest-resolution shell.

†Numbers represent the truncated data after treated with ellipsoidal truncation and anisotropic scaling.

Rmerge = ΣhklΣi|Ii(hkl)-Iav(hkl)|/ΣhklΣiIi(hkl).