TABLE 2.
Phasing and NCS averaging and refinementa
| Parameter | Value |
|---|---|
| Phasing and NCS averaging | |
| Resolution range (Å) | 24-3.2 (3.5-3.2) |
| Figure of meritb | |
| Acentric | 0.396 (0.166) |
| Centric | 0.317 (0.063) |
| Correlation coefficientc | 0.952 (0.944) |
| Refinement | |
| Resolution range (Å) | 24-2.8 (3.0-2.8) |
| No. of unique reflections | 6,153 (783) |
| R factor (%)d | 27.9 (45.8) |
| R free (%) | 37.3 (58.7) |
| Protein model | 1,846 atoms, 232 residues |
| Solvent | 0 |
| Nonprotein atoms | 0 |
| r.m.s.d. bond lengths (Å)e | 0.015 |
| r.m.s.d. angles (°)e | 1.7 |
| r.m.s.d. B (bonded) (Å2)f | 2.1, 2.8 |
| r.m.s.d. B (angle-related) (Å2)f | 3.6, 4.5 |
| Mean overall B-factor (Å2) | 79 |
a
Refinement was performed against a composite data set based on the average of all of the data for the three wavelengths. The values shown in parentheses are for the highest-resolution shell.
b
The figure of merit is derived from SHARP (9) in the absence of solvent flattening or NCS constraints.
c
The correlation coefficient is for Fs from the end of the NCS averaging.
d
R=100×Σh‖Fh,obs|−|Fh,calc‖/Σh|Fh,obs|, where Fh,obs is the observed structure factor amplitude and Fh,calc is that which has been calculated from the refined model.
e
r.m.s.d. from ideal bond lengths or bond angles.
f
r.m.s.d. of B factors for the bond or angle restraints, for main chain and side chain, respectively.