Table 1.
Statistics for crystallographic structure determination of SBP
| Data collection | |
| Wavelength (Å) | 0.996 |
| Resolution range (Å) | 11–2.80 |
| Observations | 175095 |
| Unique reflections | 26929 |
| Completeness (%)a | 88.2 (69.3) |
| Rsym (%)a,b | 9.6 (28.7) |
| Refinement | |
| Resolution range (Å) | 11–2.80 |
| Unique reflections (I > 0) | 25330 |
| Rcryst (%)c | 26.7 |
| Rfree (%)d | 29.5 |
| Number of nonhydrogen atoms | |
| Protein | 4658 |
| Solvent | 12 |
| Heterogen atoms | 45 |
| R.m.s. deviations from ideal values | |
| Bond length (Å) | 0.006 |
| Bond angle (°) | 1.1 |
| Estimated coordinate error (Å) | |
| Luzzati plote | 0.45 |
| Ramachandran plotf | |
| Residues in most favoured (disallowed: Asp256) regions (%) | 82.3 (0.8) |
| mean B-factor (Å2) | |
| Protein | 18.3 |
| Haem | 11.1 |
| Tris | 41.1 |
| Solvent | 11.18 |
a Numbers in parenthesis are for the highest resolution shell, 2.85–2.80 Å.
b Rsym = Σhkl(Σi(|Ihkl,i − <Ihkl>|)) / Σhkl,i<Ihkl>, where Ihkl,i is the intensity of an individual measurement of the reflection with Miller indices h, k, and l, and <Ihkl> is the mean intensity of that reflection.
c Rcryst = Σhkl(∥Fo,hkl| − |Fc,hkl∥) / Σhkl|Fo,hkl|, where |Fo,hkl| and |Fc,hkl| are the observed and calculated structure factor amplitudes.
dRfree is equivalent to the R-factor, but calculated with reflections omitted from the refinement process (5% of reflections omitted).
e Calculated with the program CNS (Brünger et al. 1998).
f Calculated with the program PROCHECK (Laskowski et al. 1993).