Table 1. X-ray data collection and refinement statistics for PrTX-I/RA.
| Unit cell (Å) | a = 49.4, b = 67.0, c = 85.5 |
| Space group | P212121 |
| Resolution (Å) | 40-1.77 (1.86-1.77)a |
| Unique reflections | 26992 (3895)a |
| Completeness (%) | 95.1 (97.5)a |
| Rmerge b (%) | 6.8 (41.2)a |
| Radiation source | Synchrotron (MX2 station, LNLS) |
| I/σ(I) | 16.5 (2.0)a |
| Matthews coefficient VM (Å3/Dalton) | 2.62 |
| Molecules in asymmetric unit | 2 |
| Solvent content (%) | 53.12 |
| Rcryst c (%) | 16.0 |
| Rfree d (%) | 21.7 |
| Mean B-factor (Å2)e | |
| Overall | 37.2 |
| Protein | 22.7 |
| RA molecule | 44.2 |
| R.m.s. deviations from ideal valuese | |
| bond lengths (Å) | 0.022 |
| bond angles (o) | 2.0 |
| Ramachandran plotf | |
| residues in most favorable/additionally allowed region (%) | 89.9/9.1 |
| residues in generously/not allowed regions (%) | 1.0/0 |
| Coordinate error (Å) | |
| SIGMAA (cross-validated SIGMAA)e | 0.07 (0.08) |
a
Numbers in parenthesis are for the highest resolution shell.
b
Rmerge = 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. 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 REFMAC [67].
f
Calculated with the program PROCHECK [69].