Table 1. Data-collection and refinement statistics.
Values in parentheses are for the highest-resolution shell.
| Protein | Apo MICU1–MICU2 heterodimer |
| PDB ID | 6le5 |
| Data collection | |
| Space group | P21 |
| X-ray source† | PAL-7A |
| Detector | ADSC Q270 |
| Wavelength (Å) | 0.9792 |
| Unit-cell dimensions a, b, c (Å) | 62.97, 173.72, 148.00 |
| Resolution range (Å) | 86.86–3.10 (3.18–3.10) |
| R merge ‡ | 0.256 (1.898) |
| CC1/2 (%)§ | 0.992 (0.258) |
| 〈I/σ(I)〉 | 6.2 (1.1) |
| Completeness (%) | 100.0 (100.0) |
| Redundancy | 7.2 (7.3) |
| Refinement | |
| Resolution range (Å) | 50.01–3.10 |
| No. of reflections | 54709 |
| R work (%)/R free (%)¶ | 29.3/33.2 |
| No. of atoms/residues of protein | 17392/2217 |
| B factors (Å2) of protein | 75.7 |
| Model statistics | |
| RMSD bond lengths (Å) | 0.01 |
| RMSD bond angles (°) | 1.34 |
| Ramachandran plot (%) | |
| Favored/allowed/disallowed | 93.8/6.2/0.0 |
†
Beamline 7A at the PAL in South Korea.
‡
R merge = ∑h∑i |I(h)i−〈I(h)〉|/[∑h∑i I(h)i], where I(h) is the intensity of reflection of h, ∑h is the sum over all reflections and ∑i is the sum over i measurements of reflection h.
§
CC1/2 was calculated from MOSFLM (Battye et al., 2011 ▸).
¶
R work = ∑hkl ||F o| − |F c||/(∑hkl |F o|); 5% of the reflections were excluded for the R free calculation.