Table 2.
X-ray diffraction data collection and refinement statistics for vimentin coil 1B.
| Data collection | |
| Space group | P21 |
| Unit cell dimensions | |
| a, b, c (Å) | 39.99, 77.27, 123.39 |
| α, β, γ (°) | 90, 95.03, 90 |
| Solvent content fraction | 0.47 |
| Resolution (Å) | 65.42–2.25 (2.32–2.25)a |
| <I/σ I> | 7.20 (3.50) |
| Completeness (%) | 89.8 (82.2) |
| Multiplicity | 3.0 (3.0) |
| Rmerge | 0.089 (0.305) |
| Rmeas | 0.124 (0.428) |
| CC1/2 | 0.994 (0.888) |
| Number of unique reflections | 32,022 |
| Structure refinement statistics | |
| Number of monomers per asymmetric unit | 8 |
| Resolution (Å) | 40.97–2.25 |
| Rwork (%) | 23.5 |
| Rfree (%) | 28.2 |
| R.m.s.d. from ideal | |
| bond lengths deviation (Å) | 0.007 |
| bond angles deviation (°) | 0.83 |
| Number of protein atoms | 5340 |
| Average B-factors (Å2) | |
| protein | 38 |
| water | 44 |
| glycerol | 51 |
| % of residues in | |
| favored regions | 99.25 |
| allowed regions | 0.75 |
| outlier regions | 0.00 (0 residues) |
a
Numbers in parentheses indicate the values in the highest-resolution shell.
b
Indicates MolProbity [47] statistics.