TABLE 2.
Data collection and refinement statistics for fucosylated and afucosylated human Fc from N. benthamianaa
| Parameter | Fucosylated human Fc | Afucosylated human Fc |
|---|---|---|
| Data collection | ||
| Wavelength (Å) | 0.920 | 0.979 |
| Space group | P212121 | P212121 |
| Cell parameters | ||
| a, b, c (Å) | 49.9, 79.9, 138.5 | 49.7, 80.3, 137.0 |
| α, β, γ (°) | 90, 90, 90 | 90, 90, 90 |
| Fcs/a.u. | 1 | 1 |
| Resolution (Å) | 50–2.1 (2.21–2.1) | 50–2.6 (2.74–2.6) |
| No. of reflections | ||
| Total | 106,578 | 54,596 |
| Unique | 32,561 | 15,294 |
| Rmergeb (%) | 9.7 (77.5) | 8.3 (90.2) |
| Rpimc (%) | 6.1 (47.9) | 4.7 (49.7) |
| CC1/2d | 0.99 (0.50) | 0.99 (0.68) |
| I/σ | 5.4 (1.0) | 8.3 (1.8) |
| Completeness (%) | 98.7 (99.3) | 88.0 (90.2) |
| Redundancy | 3.3 (3.4) | 3.6 (3.6) |
| Refinement statistics | ||
| Resolution (Å) | 50.0–2.1 | 50.0–2.6 |
| Re (%) | 20.8 | 22.1 |
| Rfreef (%) | 25.0 | 27.6 |
| No. of atoms | ||
| Protein | 3,359 | 3,335 |
| Water | 189 | 20 |
| Ligand/glycan | 236 | 200 |
| Overall B value (Å)2 | ||
| Protein | 59 | 81 |
| Water | 48 | 46 |
| Ligand/ion | 80 | 102 |
| RMSDg | ||
| Bond lengths (Å) | 0.010 | 0.014 |
| Bond angles (°) | 1.1 | 1.6 |
| Ramachandran (%)h | ||
| Favored | 96.6 | 90.3 |
| Allowed | 2.9 | 5.8 |
| Outliers | 0.5 | 3.9 |
| PDB ID | 6VSL | 6VSZ |
a
Values in parentheses are for highest-resolution shell.
b
Rmerge = ∑|I – 〈I〉|/∑I, where I is the observed intensity and is the average intensity obtained from multiple observations of symmetry-related reflections after rejections.
c
Rpim = as defined by Weiss (88).
d
CC1/2 is as defined by Karplus and Diederichs (89).
e
R = ∑||Fo|–|Fc||/∑|Fo|, where Fo and Fc are the observed and calculated structure factors, respectively.
f
Rfree = as defined by Brünger (90).
g
RMSD, root mean square deviation.
h
Calculated with MolProbity.