Table 3. Summary of crystal parameters, data-collection and refinement statistics for Q9HJ63_THEAC (PDB entry 2gvi).
Values in parentheses are for the highest resolution shell.
| λ1 | |
|---|---|
| Space group | I222 |
| Unit-cell parameters (Å) | a = 78.60, b = 97.65, c = 75.27 |
| Data collection | |
| Wavelength (Å) | 1.000 |
| Resolution range (Å) | 30.08–1.87 (1.94–1.87) |
| No. of observations | 92701 |
| No. of unique reflections | 24247 |
| Completeness (%) | 99.8 (99.9) |
| Mean I/σ(I) | 10.5 (1.7) |
| Rmerge on I† (%) | 10.3 (83.1) |
| Rmeas on I‡ (%) | 12.0 (96.8) |
| Model and refinement statistics | |
| Resolution range (Å) | 30.1–1.87 |
| No. of reflections (total) | 24246 |
| No. of reflections (test) | 1229 |
| Completeness (%) | 99.7 |
| Cutoff criterion | |F| > 0 |
| Rcryst | 0.190 |
| Rfree | 0.217 |
| Stereochemical parameters | |
| Restraints (r.m.s.d. observed) | |
| Bond angles (°) | 1.64 |
| Bond lengths (Å) | 0.014 |
| Average isotropic B value (Å2) | 31.1 |
| ESU based on Rfree (Å) | 0.12 |
| Protein residues/atoms | 201/1599 |
| Waters/solvent molecules/ions | 129/15/5 |
†
R
merge = 
, where I
i(hkl) is the scaled intensity of the ith measurement and 〈I(hkl)〉 is the mean intensity for that reflection.
§
R
cryst = 
, where F
calc and F
obs are the calculated and observed structure-factor amplitudes, respectively.
¶
R free is the same as R cryst but for 5.1% of the total reflections chosen at random and omitted from refinement.