Statistics of X-ray diffraction data and structure refinement
| Data collection . | cβ3-E2-P33 . | cβ3-E2-L33 . | |
|---|---|---|---|
| Before dehydration . | After dehydration . | No dehydration . | |
| Space group | P21 | P21 | P21 |
| Unit cell | |||
| a, b, c, Å | 59.08, 80.91, 126.72 | 59.56, 79.84, 116.16 | 59.07, 81.47, 127.96 |
| α, β, γ, ° | 90.0, 96.4, 90.0 | 90.0, 91.42, 90.0 | 90.0, 97.1, 90.0 |
| Wavelength, Å | 0.97872 | 0.97872 | 0.97872 |
| Resolution, Å | 2.80 | 2.39 | 3.20 |
| Rmerge, %*† | 15.0 (>100) | 13.8 (>100) | 22.6 (>100) |
| No. of reflections, measured/unique | 222 851/29 474 | 328 778/43 236 | 152 292/20 112 |
| I/σ(I)* | 8.6 (0.5) | 9.6 (0.7) | 6.5 (0.6) |
| Completeness, %* | 100 (100) | 99.7 (98.8) | 100 (100) |
| Redundancy* | 7.6 (7.6) | 7.6 (6.8) | 7.6 (7.6) |
| CC1/2* | 0.995 (0.118) | 0.996 (0.121) | 0.959 (0.134) |
| Refinement | |||
| Resolution, Å | 2.80 | 2.39 | 3.20 |
| Unique reflections, work/free | 29 394/1 479 | 43 143/2 128 | 20 063/1 019 |
| Rwork/Rfree‡ | 0.242/0.296 | 0.219/0.267 | 0.265/0.335 |
| No. of atoms, protein/carbohydrates/water | 7 223/70/4 | 7 215/70/170 | 7 197/98/8 |
| Molecules per asymmetric unit | 2 | 2 | 2 |
| RMSD from ideal | |||
| Bond lengths, Å | 0.009 | 0.004 | 0.003 |
| Bond angles, ° | 1.052 | 0.650 | 0.625 |
| Ramachandran plot, favored/allowed/outliers, % | 87.57/10.81/1.62 | 92.64/7.14/0.22 | 87.87/9.75/2.38 |
| PDB code | 6CKB | 6BXB | 6BXF |
| Data collection . | cβ3-E2-P33 . | cβ3-E2-L33 . | |
|---|---|---|---|
| Before dehydration . | After dehydration . | No dehydration . | |
| Space group | P21 | P21 | P21 |
| Unit cell | |||
| a, b, c, Å | 59.08, 80.91, 126.72 | 59.56, 79.84, 116.16 | 59.07, 81.47, 127.96 |
| α, β, γ, ° | 90.0, 96.4, 90.0 | 90.0, 91.42, 90.0 | 90.0, 97.1, 90.0 |
| Wavelength, Å | 0.97872 | 0.97872 | 0.97872 |
| Resolution, Å | 2.80 | 2.39 | 3.20 |
| Rmerge, %*† | 15.0 (>100) | 13.8 (>100) | 22.6 (>100) |
| No. of reflections, measured/unique | 222 851/29 474 | 328 778/43 236 | 152 292/20 112 |
| I/σ(I)* | 8.6 (0.5) | 9.6 (0.7) | 6.5 (0.6) |
| Completeness, %* | 100 (100) | 99.7 (98.8) | 100 (100) |
| Redundancy* | 7.6 (7.6) | 7.6 (6.8) | 7.6 (7.6) |
| CC1/2* | 0.995 (0.118) | 0.996 (0.121) | 0.959 (0.134) |
| Refinement | |||
| Resolution, Å | 2.80 | 2.39 | 3.20 |
| Unique reflections, work/free | 29 394/1 479 | 43 143/2 128 | 20 063/1 019 |
| Rwork/Rfree‡ | 0.242/0.296 | 0.219/0.267 | 0.265/0.335 |
| No. of atoms, protein/carbohydrates/water | 7 223/70/4 | 7 215/70/170 | 7 197/98/8 |
| Molecules per asymmetric unit | 2 | 2 | 2 |
| RMSD from ideal | |||
| Bond lengths, Å | 0.009 | 0.004 | 0.003 |
| Bond angles, ° | 1.052 | 0.650 | 0.625 |
| Ramachandran plot, favored/allowed/outliers, % | 87.57/10.81/1.62 | 92.64/7.14/0.22 | 87.87/9.75/2.38 |
| PDB code | 6CKB | 6BXB | 6BXF |
PDB, Protein Data Bank; RMSD, root mean square deviation.
The highest-resolution shell is shown in parentheses.
Rmerge = ∑h∑i|Ii − 〈I〉|/∑h∑iIi, where Ii is the observed intensity of the i-th measurement of reflection h, and 〈I〉 is the average intensity of that reflection obtained from multiple observations.
R = ∑||Fo| − |Fc||/∑|Fo|, where Fo and Fc are the observed and calculated structural factors, respectively, calculated for all data. Rfree is the R value obtained for a test set of reflections consisting of a randomly selected ∼5% subset of data excluded from refinement.