Table 1.
Crystallographic data, phasing and refinement statistics
| Structure | Mini spindles TOG2 | Stu2p TOG2 | EB1 CH Domain | Bim1p CH Domain | CLIP-170 CG 1 | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Space group | C2221 | P212121 | P21 | P212121 | P21212 | ||||||||||
| Cell: a,b,c (Å) | 91.4, 113.4, 78.6 | 28.4, 80.6, 97.2 | 29.3, 65.2, 63.1 (β = 96.2°) | 35.8, 102.5, 31.3 | 27.2, 42.5, 51.8 | ||||||||||
| Wavelength (Å) | 0.97963 | 0.97974 | 1.00801 | 0.97959 | 0.97972 | 1.01627 | 1.12714 | 0.9798 | 1.1271 | 0.7999 | 0.97962 | 0.97979 | 1.03320 | 0.97964 | 1.12713 |
| dmin (Å) | 2.10 | 2.10 | 2.10 | 2.10 | 2.10 | 2.10 | 1.70 | 1.50 | 1.50 | 1.25 | 1.90 | 1.90 | 1.90 | 2.00 | 2.00 |
| % Complete | 97.5 (96.5) |
98.6 (96.4) |
98.2 (91.6) |
97.2 (87.4) |
98.1 (87.4) |
96.1 (87.4) |
99.0 (94.6) |
94.1 (68.7) |
84.9 (31.9) |
97.4 (95.7) |
98.6 (98.5) |
99.7 (98.8) |
98.2 (85.9) |
99.7 (100.0) |
99.4 (99.9) |
| I/σ | 24.6 (3.6) |
25.5 (3.7) |
27.7 (4.3) |
25.2 (6.4) |
23.1 (2.4) |
25.4 (6.1) |
25.5 (9.4) |
20.8 (2.6) |
26.3 (5.2) |
14.9 (3.2) |
33.2 (17.9) |
35.6 (16.2) |
39.3 (12.4) |
22.7 (14.9) |
20.9 (15.0) |
| Rsym (%) * | 3.9 (24.0) |
3.8 (22.9) |
3.5 (18.5) |
4.4 (9.2) |
4.3 (8.9) |
3.9 (7.8) |
4.0 (9.7) |
4.9 (31.5) |
3.5 (14.3) |
5.4 (32.1) |
4.1 (6.7) |
3.9 (7.5) |
3.4 (6.8) |
4.8 (9.2) |
4.6 (7.9) |
|
Phasing power† + Friedel / - Friedel |
1.69 (0.55) / 1.92 (0.61) |
1.99 (0.62) / 2.14 (0.67) |
Ref / 0.27 (0.07) |
2.37 (1.30) / 2.68 (1.48) |
2.92 (1.53) / 3.13 (1.65) |
Ref / 0.47 (0.24) |
3.25 (1.36) / 3.38 (1.46) |
Ref / 0.65 (0.28) |
1.25 (1.16) / 1.50 (1.27) |
2.65 (1.62) / 2.85 (1.69) |
Ref / 0.44 (0.20) |
1.28 (0.87) / 1.37 (0.88) |
Ref / 0.24 (0.07) |
||
|
Figure of merit◇ Centrics / Acentrics |
0.78(0.46) / 0.61(0.25) | 0.87(0.74) / 0.79(0.55) | 0.82(0.76) / 0.72(0.41) | 0.89(0.70) / 0.76(0.58) | 0.72(0.65) / 0.44(0.34) | ||||||||||
| Refinement (Å) | 500-2.10 | 500-1.70 | 500-1.25 | 500-1.90 | 500-2.00 | ||||||||||
| R value ‡ | 20.2 (23.5) | 17.3 (18.7) | 17.4 (19.0) | 19.3 (19.2) | 17.3 (16.2) | ||||||||||
| Rfree § | 21.7 (25.8) | 19.6 (22.6) | 19.8 (21.5) | 22.5 (22.8) | 23.3 (21.3) | ||||||||||
| Rmsd bond lengths (Å) | 0.005 | 0.005 | 0.008 | 0.005 | 0.005 | ||||||||||
| Rmsd bond angles (°) | 1.09 | 1.16 | 1.03 | 1.16 | 1.29 | ||||||||||
| Mean B (min / max) (Å2) | 34.0 (15.0 / 87.7) | 17.2 (5.7 / 59.0) | 12.3 (4.3 / 61.6) | 22.1 (3.9 / 56.1) | 11.2 (1.5 / 51.2) | ||||||||||
| No. protein / solvent atoms | 1852 / 161 | 1991 / 314 | 1974 / 304 | 991 / 101 | 572 / 66 | ||||||||||
Values in parentheses are for the highest resolution shells unless otherwise denoted.
where Ii(h) is the integrated intensity of the ith reflection with the Miller Index h and <I(h)> is the average over Friedel and symmetry equivalents.
MAD phasing power is defined as where P(ϕ) is the experimental phase probability distribution. FN are structure factors at the designated reference wavelength and FD are structure factors of + or - Friedel mates at the other designated wavelength. ΔFh is the difference in heavy atom structure factors between two wavelengths.
Figure of merit is the weighted mean of the cosine of the deviation from αbest.
R value = .
Rfree is calculated using a 10% subset of the data that is removed randomly from the original data and excluded from refinement.