TABLE 1.
Crystallographic data collection, phasing, and refinement statistics for the catalytic domain of Rat CCTα
The data collection statistics in parentheses are the values for the highest resolution shell. Se-Met is selenomethionine.
| Native | Se-Met incorporated | |
|---|---|---|
| Crystal parameters | ||
| Space group | P21212 | P2 |
| a, b, c | 89.0, 129.4, 43.6 Å | 129.2, 43.8, 88.3 Å |
| α, β, γ | 90.0, 90.0, 90.0° | 90.0, 90.02, 90.0° |
| Data collection statistics | ||
| Wavelength | 1.00 Å | 0.9795 Å |
| Resolution | 50.0-2.2 Å (2.28-2.20 Å) | 50.0-3.5 Å (3.63-3.50 Å) |
| Total reflections | 294,978 | 88,104 |
| Unique reflections | 26,316 | 12,964 |
| Rmergea | 0.105 (0.326) | 0.163 (0.269) |
| Mean (I)/σI | 32.7 (6.6) | 14.1 (6.8) |
| Completeness | 100.0% (100.0%) | 99.8% (99.8%) |
| Redundancy | 11.2 (10.6) | 6.4 (6.8) |
| Phasing statistics | ||
| No. of sites | 17 (out of possible 20) | |
| Overall FOMb | 0.24 | |
| Overall FOM (after density modification) | 0.63 | |
| Refinement statistics | ||
| Protein molecules in asymmetric units | 2 | |
| Residues | 353 | |
| Water molecules | 249 | |
| Total no. of atoms | 3176 | |
| Rcrystc/Rfreed | 0.22/0.27 | |
| Average B-factor (all atoms) | 27.7 Å2 | |
| Average B-factor (CDP-choline) | 19.1 Å2 | |
| r.m.s.d. on angles | 2.08° | |
| r.m.s.d. on bonds | 0.03 Å | |
a Rmerge = ΣhklΣi|Ii(hkl)− I¯(h¯k¯l¯)|/ΣhklΣiIi(hkl), where Ii(hkl) is the observed intensity, and I¯(h¯k¯l¯) is the average intensity obtained from multiple observations of symmetry-related reflections after rejections.
b FOM is figure of merit; 〈|ΣP(α)eiα/ΣP(α)|〉, where α is the phase angle and P(α) is the phase probability distribution.
c Rcryst = Σ‖Fo| − |Fc‖/Σ|Fo|, where Fo and Fc are the observed and calculated structure factors, respectively.
d Rfree is calculated using 5% of the reflections randomly excluded from refinement.