Table 1.
Structure Determination
| Diffraction Data Statistics | AvrL567-A | AvrL567-D |
|---|---|---|
| Resolution (Å) | 50.0–1.43 (1.468–1.432)a | 50.0–2.26 (2.316–2.262)a |
| Observations | 337,806 | 102,320 |
| Unique reflections | 28,149 | 7,619 |
| Completeness (%) | 99.1 (93.3) | 99.7 (98.5) |
| Rmerge (%)b | 0.056 (0.238) | 0.113 (0.497) |
| Average I/σ(I) | 33.7 (13.95) | 11.9 (8.35) |
| Refinement statistics | ||
| Resolution (Å) | 42.1–1.43 (1.468–1.432) | 40.26–2.26 (2.316–2.262) |
| Number of reflections | 26,436 | 7,199 |
| Rcrystc | 0.220 (0.387) | 0.195 (0.240) |
| Rfreed | 0.254 (0.384) | 0.257 (0.352) |
| Number of nonhydrogen atoms: | ||
| Protein | 1104 | 913 |
| Solvent | 199 | 103 |
| Mean B-factor (Å2) | 24.6 | 28.4 |
| Coordinate error (Å) | 0.198 | 0.250 |
| Root mean square deviations from ideal values: | ||
| Bond lengths (Å) | 0.015 | 0.019 |
| Bond angles (°) | 1.617 | 1.702 |
| Ramachandran plot: | ||
| Residues in most favored (disallowed) regions (%)e | 88.9 (0) | 87.9 (0) |
a
Numbers in parenthesis are for the highest resolution shell.
b
Rmerge = ∑hkl(∑i(|I hkl,i − <I hkl >|))/∑hkl,i <I hkl>, where I hkl,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. Calculated for I > −3σ(I).
c
Rcryst = ∑hkl(‖Fobshkl| − |Fcalchkl‖)/|Fobshkl|, where |Fobshkl| and |Fcalchkl| are the observed and calculated structure factor amplitudes.
d
Rfree is equivalent to Rcryst but calculated with reflections (5%) omitted from the refinement process.
e
Calculated with the program PROCHECK (Laskowski et al., 1993).
fCalculated based on the Luzzati plot with the program SFCHECK (Vaguine et al., 1999).