Table 1.
Summary of data-collection and refinement statistics for MIP-2.
| Data statistics | |
| Space group | P212121 |
| Unit-cell parameters (Å) | |
| a | 41.76 |
| b | 59.45 |
| c | 99.35 |
| Resolution (Å) | 1.9 |
| No. of reflections | 101689 |
| Unique reflections | 20213 |
| Completeness (%) | 99.9 (100) |
| Redundancy | 5.0 (5.0) |
| Rmerge (%)a | 3.9 (10.1) |
| I/σ(I) | 30.443(14.927) |
| Solvent content (%) | 37 |
| No of Protein molecules in ASU | 4 |
| Refinement statistics | |
| No. of reflections | 19059 |
| Rfactor (%)b | 18.7 |
| Rfree (%)b | 22.5 |
| No. of protein atoms | 2038 |
| No. of water molecules | 263 |
| Average B factors (Å2) | 45.6 |
| R.m.s.d. from ideal values | |
| Bond lengths (Å) | 0.030 |
| Bond angles (°) | 2.459 |
| Ramachandran statistics (%) | |
| Most favored | 96.5 |
| Favored | 3.5 |
| Additionally allowed | |
| Disallowed | |
Values in parentheses are for the high-resolution shell (1.97–1.90Å).
a
Rmerge = 100×ΣhΣi|(h)l−〈(h)〉|/ΣhΣi〈(hi)〉, where I is the observed intensity, and 〈I〉 is the average intensity of multiple observations of symmetry-related reflections.
c
R = Σ||Fo|−|Fc||/Σ|Fo|. Rfactor and Rfree were calculated using the working and test reflection sets, respectively. 5% of the entire reflection was randomly taken as a test set.