Table 1 Crystallographic data collection and refinement
From: Structural insights of human mitofusin-2 into mitochondrial fusion and CMT2A onset
State | MFN2IM | MFN2IM | MFN2IM(T111D) |
|---|---|---|---|
apo | GDP | apo | |
Data collection | |||
 Space group | P1211 | P41212 | P1211 |
 Cell dimensions | |||
 a, b, c (Å) | 84.5, 128.4, 91.3 | 49.6, 49.6, 388.1 | 44.4, 126.6, 78 |
 α, β, γ (°) | 90, 106.3, 90 | 90 | 90, 102.5, 90 |
 Wavelength (Å) | 0.97915 | 0.977760 | 0.97914 |
 Resolution (Å) | 48.7–2.8 (2.98–2.81) | 49.6–2.0 (2.12–2.00) | 126.6–2.1 (2.14–2.09) |
 R sym a | 0.106 (0.490) | 0.058 (0.475) | 0.070 (0.573) |
 I/σ(I) | 10.42 (3.05) | 18.31 (3.22) | 10.6 (2.2) |
 Completeness (%) | 98.0 (94.5) | 99.3 (98.2) | 98.8 (99.5) |
 Redundancy | 3.3 (3.3) | 6.2 (5.9) | 4.4 (4.3) |
Refinement | |||
 Resolution (Å) | 36.3–2.8 | 48.1–2.0 | 31.6–2.1 |
 No. reflections | 44910 | 34449 | 50316 |
 Rwork/Rfree | 0.207/0.283 | 0.176/0.212 | 0.176/0.229 |
 No. atoms | |||
 Protein | 13347 | 3424 | 6824 |
 Ligand/ion | 7 | 65 | 11 |
 Water | 132 | 171 | 268 |
B-factors | |||
 Protein | 52.3 | 43.9 | 45.5 |
 Ligand/ion | 71.2 | 51.0 | 61.2 |
 Water | 39.6 | 46.2 | 48.9 |
R.m.s. deviations | |||
 Bond lengths (Å) | 0.009 | 0.007 | 0.008 |
 Bond angles (°) | 1.184 | 0.903 | 0.943 |
