Table 1.
Data collection and refinement statistics
| Structure of fascin bound with NP- G2-029 a | |
|---|---|
| Native PDB 6B0T | |
| Data collection | |
| Space group | P2 |
| Cell dimensions | |
| a, b, c (Å) | 102.58, 59.25, 293.65 |
| α β γ (°) | 90, 90.02, 90 |
| Resolution (Å) | 45.44-2.8 (2.9-2.8) b |
| Number of reflections measured | 364035 (36079) |
| Number of unique reflections | 87042 (8516) |
| Rmerge | 0.09 (0.44) |
| I / σ (I) | 13.59 (3.46) |
| Completeness (%) | 99.0 (98.0) |
| Redundancy | 4.2 (4.2) |
| Refinement | |
| Resolution (Å) | 45.44-2.8 |
| No. reflections (test set) | 87025 (4264) |
| Rwork / Rfree (%) | 26.51/30.28 |
| Number of non-hydrogen atoms | |
| Protein | 22818 |
| Ligand | 174 |
| Water | 344 |
| Mean overall B factor (Å2) | 67.4 |
| Wilson B | 38.2 |
| Protein | 67.7 |
| Ligand | 76.6 |
| Water | 43.8 |
| r.m.s. deviations | |
| Bond lengths (Å) | 0.003 |
| Bond angles (°) | 0.59 |
| Ramachandran plot statisticsc (%) | |
| Favored regions | 91.3 |
| Allowed regions | 8.1 |
| Disallowed regions | 0.6 |
a
One single crystal was used for data collection and refinement.
b
Values in parentheses are for highest-resolution shell.
c
As defined in MolProbity.