Table 1.
Data collection, structure determination, and refinement statistics for the X-ray crystal structure of the CT domain of MCAK bound to its motor domain
| Statistics | MCAK motor domain-peptide complex |
|---|---|
| Unit cell dimensions | a = 46.31 Å, b = 245.64 Å, c = 79.40 Å, α = 90.00°, β = 95.84°, γ = 90.00° |
| Space group | P21 |
| Molecules per asymmetric unit | 4 |
| Resolution range (Å) | 30.0–3.0 |
| Total reflections | 155983 |
| Unique reflections | 35,146 |
| Completeness (%) | 99.0 (99.2) |
| Multiplicity | 4.4 (4.5) |
| Rsym (%) | 9.1 (68.2) |
| I/σ(I) | 10.2 (2.0) |
| Rwork/Rfree (%) | 26.4/28.6 |
| Wilson B (Å2) | 77.5 |
| Average B (Å2): | |
| Overall | 71.0 |
| Main chain | 72.05 |
| Side chain and solvent | 70.66 |
| Peptide | 56.98 |
| r.m.s.d. bond lengths (Å) | 0.095 |
| r.m.s.d. bond angles (°) | 1.53 |
| Ramachandran plot statistics (%): | |
| Favoured | 87.6 |
| Allowed | 11.7 |
| Outliers | 0.7 |