Table 2. Crystallographic data and refinement statistics.
| SeMet | Native | |
| Diffraction data a | ||
| Space group | P3121 | P3121 |
| Cell dimensions: a, c (Å) | 128.88, 126.66 | 127.95, 127.25 |
| Resolution (Å) | 20.00−2.80 (2.90−2.80)b,c | 30.00−2.84 (2.94−2.84) |
| Unique HKLs | 27,466 (984) | 29,072 (2,860) |
| Completeness (%) | 90.7 (32.8) | 100.0 (100.00) |
| Rsym d (%) | 14.7 (>1) | 8.9 (97.8) |
| <I/σI> | 20.5 (0.4) | 40.0 (3.0) |
| Redundancy | 8.1 (1.5) | 11.1 (10.5) |
| Refinement | ||
| Initial phasing mean FOMe | - | 0.30 |
| No. of atoms: protein/others | - | 5,885/3 |
| Rwork/Rfree f (%) | - | 20.5/24.5 |
| Coordinate errorg Rwork/Rfree/max likelihood (Å) | - | 0.71/0.32/0.29 |
| RMSD bond length (Å)/angle (°) | - | 0.012/1.1 |
| Mean B-factor (Å2) | - | 73.8 |
| Ramachandran plot favored/outliers (%) | - | 96.1/0.0 |
a
Data reduced with DENZO and SCALEPACK.
b
Numbers in parentheses are for outer shell.
c
Phasing data were complete only to 3.15 Å, but were not re-scaled to that resolution limit.
d
Rsym = Σ|I-<I>|/ΣI.
e
FOM: Figures of merit.
f
Rwork = Σ||Fo|−|Fc||/Σ|Fo|, where Fo and Fc are the observed and calculated structure factors, respectively. Rfree was calculated as Rwork by using 3.8% of the data selected in thin resolution shells with SFTOOLS.
g
Estimated standard coordinate uncertainty.