Table 1.
X-ray data collection and refinement statisticsa
| Name | Hb(ONO)d,p | NαHb(ONO) | NHb(ONO)α |
|---|---|---|---|
| PDB Accession Code | 3ONZ | 3OO4 | 3OO5 |
| A. Crystal parameters | |||
| Space group | P41212 | P41212 | P41212 |
| Unit cell dimensions (Å) | 53.3, 53.3, 193.6 | 53.5, 53.5, 190.0 | 53.5, 53.5, 192.2 |
| Molecules per asymmetric unit | α1β1 | α1β1 | α1β1 |
| Solvent content (%) | 42.3 | 45.3 | 44.5 |
| B. Data collection | |||
| Wavelength (Å) | 1.5418 | 1.5418 | 1.5418 |
| Temperature (K) | 100 | 100 | 100 |
| Resolution range (Å) | 46.7–2.09 | 27.3–1.9 | 27.5–2.1 |
| Number of observations | 156086 | 161544 | 217415 |
| Unique reflections | 16567 | 22776 | 17257 |
| Average multiplicity | 9.4 (9.4) | 7.1 (5.23) | 12.6 (12.6) |
| Completeness (%) | 95.5 (90.7) | 100 (100) | 100 (100) |
| <I/σ(I)> | 29.3 (4.6) | 12.7 (2.0) | 14.6 (3.3) |
| Rmergeb | 0.053 (0.405) | 0.057 (0.365) | 0.053 (0.482) |
| C. Refinement | |||
| Resolution (Å) | 26.64–2.09 | 27.3–1.9 | 27.5–2.1 |
| No. of reflections used | 16540 | 22697 | 17179 |
| No. of reflections used for Rfree | 856 | 1162 | 870 |
| No. of protein atoms | 2183 | 2287 | 2244 |
| R-factorc | 0.219 | 0.207 | 0.231 |
| R free d | 0.287 | 0.263 | 0.287 |
| Wilson B (Å2) | 39.1 | 32.8 | 48.2 |
| rms deviations from ideal valuese |
|||
| Bond lengths (Å) | 0.02 | 0.01 | 0.01 |
| Bond angles (°) | 1.9 | 1.1 | 1.2 |
| Ramachandran plot (%)f | |||
| Favored region | 93.7 | 98.2 | 97.5 |
| Outliers | 0.7 | 0 | 0 |
| Rotamer outliers | 4.1 | 0.9 | 1.8 |
a
The data in brackets refer to the highest resolution shell.
b
Rmerge = ∑□∑i ∣Ihi − <Ih>∣/∑□∑i ∣<Ih>∣. Ihi is the ith used observation for unique hkl h, and <Ih> is the mean intensity for unique hkl h.
c
R = ∑∣∣Fo∣− ∣Fc∣∣/∑∣Fo∣ where Fo and Fc are the observed and calculated structure factors, respectively.
d
Rfree was calculated using 5% of the randomly selected diffraction data which were excluded from the refinement.
e
Ideal values taken from: Engh, RA & Huber, R (1991) Accurate Bond and Angle Parameters for X-ray Protein Structure Refinement. Acta Cryst. A47: 392-400.
f
calculated using MolProbity as implemented in PHENIX.