Table 1. Data collection and structure determination.
| mPrx4 C54A (full-length) (oxidized form) | P5 a0-Prx4 C-terminal peptide complex | |
|---|---|---|
| Data collection | ||
| Beamline | BL44XU at SPring-8 | BL5A at KEK |
| Space group | P21221 | P212121 |
| Cell dimensions (Å) | a = 87.5, b = 118.7, c = 255.7 | a = 39.0, b = 53.4, c = 133.4 |
| α = β = γ = 90.0° | α = β = γ = 90.0° | |
| Wavelength (Å) | 0.90000 | 1.0000 |
| Resolution range (Å) | 43.73 − 3.30 (3.38 − 3.30) | 41.67 − 2.10 (2.14 − 2.10) |
| No. of total observations | 254,583 | 112,980 |
| No. of unique reflections | 38,676 | 16,851 |
| Completeness (%) | 94.6 (88.7) | 98.9 (92.7) |
| I/σ(I) | 13.9 (4.4) | 26.0 (3.1) |
| Multiplicity | 6.6 (6.5) | 6.7 (5.7) |
| Rmergea | 0.104 (0.450) | 0.070 (0.500) |
| Refinement | ||
| Resolution range (Å) | 43.11 − 3.30 | 41.67 − 2.10 |
| Rworkb | 0.203 | 0.182 |
| Rfreec | 0.255 | 0.245 |
| RMS deviation | ||
| Bond length (Å) | 0.014 | 0.007 |
| Bond angle (°) | 1.8 | 1.0 |
| Ramachandran analysise | ||
| Most favored (%) | 98.3 | 96.4 |
| Allowed (%) | 1.7 | 3.6 |
| Generously allowed (%) | 0.0 | 0.0 |
| Disallowed (%) | 0.0 | 0.0 |
The number in parentheses represent statistics in the highest resolution shell.
aRmerge = ΣΣj|<I(h)> − I(h)j|/ΣΣj|<I(h)>|, where <I(h)> is the mean intensity of symmetry-equivalent reflections.
bRwork = Σ(IIFp(obs)I − IFp(calc)II)/ΣIFp(obs)I.
cRfree = R factor for a selected subset (5%) of the reflections that was not included in prior refinement calculations.