Table 1 Data collection and refinement statistics.
From: The structure of the FANCM–MHF complex reveals physical features for functional assembly
Data collection | ||
|---|---|---|
MHF11–107–MHF2 | MHF11–114–MHF2–FANCM-F | |
Native | SeMet | |
Space group | P21 | P21 |
Cell dimensions (Å) | ||
a, b, c (Å) | 41.01, 128.77, 88.70 | 111.32, 70.03, 115.75 |
α, β, γ (°) | 90.00, 100.74, 90.00 | 90.00, 91.41, 90.00 |
Wavelength (Å) | 0.9794 | 0.9792 |
Resolution (Å)a | 50.00–2.41 (2.45–2.41) | 50–2.64 (2.73–2.64) |
Total reflections | 125,710 | 351,195 |
Unique reflections | 32,631 (1477) | 52,925 (5221) |
Redundancy | 3.9 (3.1) | 6.6 (6.2) |
Rmerge (%)b | 7.3 (47.2) | 10.6 (45.9) |
I/ó (I) | 16.03 (2.53) | 24.31 (4.62) |
Completeness (%) | 94.1 (86.4) | 100 (100) |
Refinement | ||
Resolution | 34.15–2.41 (2.50–2.41) | 49.67–2.64 (2.73–2.64) |
Unique reflections | 31,356 (2,407) | 50,516 (4,254) |
Rwork (%)c | 19.04 (23.72) | 22.05 (27.91) |
Rfree (%)c | 24.17 (30.98) | 25.56 (33.12) |
Number of atoms | ||
Residue | 677 | 1,344 |
Protein | 5,271 | 10,388 |
Water | 116 | 120 |
B factors (Å2) | ||
Protein | 44.73 | 45.04 |
Water | 43.94 | 41.50 |
r.m.s.d. | ||
Bond lengths (Å) | 0.003 | 0.002 |
Bond angles (°) | 0.557 | 0.539 |
- aHigh-resolution shell is shown in parentheses.
- bRmerge=Σ|Ii−
|/Σ|I|, where Ii is the intensity of an individual reflection and is the average intensity of that reflection. - cRwork=Σ||Fo−|Fc||/Σ|Fo| for all reflections and Rfree=Σ||Fo−|Fc||/Σ|Fo|, calculated on the 5% of data excluded from refinement.
|/Σ|I|, where Ii is the intensity of an individual reflection and 