Table 2.
Data Collection Statistics, Determination, and Refinement for MAP_1204
| Parameters | Data collection and structure solution |
|---|---|
| Beamline | APS 22‐BM |
| Wavelength (Å) | 1.000 |
| Space group | P21 3 |
| Unit cell dimensions (Å) | a = 97.11 |
| Resolution limits (Å) | 43.43–2.40 (2.64–2.40)a |
| Completeness (%) | 99.6 (100) |
| Total reflections | 12,254 |
| Unique reflections | 1,213 |
| R merge (%)b | 16.9 (85.6) |
| ≪I>/<σ≫ | 14.1 (2.2) |
| Redundancy | 13.0 |
| Refinement statistics | |
| R cryst/R free (%)c | 22.0/28.0 |
| RMS deviations from ideality | |
| Bond length (Å) | 0.008 |
| Bond angle (°) | 1.21 |
| Dihedral angle (°) | 16.995 |
| Ramachandran core (disallowed) (%) | 91.1 (1.9) |
| Average B factor (Å2) | 30.21 |
| RMSD of B factor (Å2) | 7.72 |
| Proteins atoms modeled | 2042 |
| Ordered solvent molecules | 45 |
a
Numbers in parentheses correspond to the highest resolution shell.
b
R merge = Σh Σi|I i(h) − <I(h)>|/Σh Σi I i(h), where I i(h) is the i th measurement of reflection h and <I(h)> is the weighted mean of all measurements of h.
c
R = Σh|F obs(h) − F calc(h)|/Σh ΣF obs|. R cryst and R free were calculated from the working and test reflection sets, respectively. The test set constituted 5% of the total reflections not used in refinement.