Table 1.
X-ray diffraction data collection, phasing, and refinement statistics for αTSR structure
| Protein Data Bank deposition code* |
|||
| 3VDJ | 3VDK | 3VDL | |
| Data collection | |||
| Space group | H32 | H32 | P43212 |
| Molecules/asymmetric unit | 1 | 1 | 3 |
| Cell dimensions | |||
| a, b, c (Å) | 66.52, 66.52, 85.51 | 66.53, 66.53, 86.49 | 63.37, 63.37, 118.16 |
| α, β, γ (°) | 90, 90, 120 | 90, 90, 120 | 90, 90, 90 |
| Wavelength, Å | 0.97949 | 1.07195 | 0.97949 |
| Resolution, Å | 50–1.70 (1.73–1.70)† | 50–1.85 (1.92–1.85)† | 50–2.04 (2.11–2.04)† |
| Observations (unique) | 40,160 (8,160) | 41,336 (6,375) | 176,960 (15,611) |
| I/σ overall | 22.7 (3.6) | 42.6 (2.9) | 21.6 (1.44) |
| Completeness | 99.1 (91.1) | 98.1 (86.9) | 97.1 (74.7) |
| Rmerge‡ | 5.7 (35.1) | 9.1 (64.3) | 9.6 (69.4) |
| SAD phasing | |||
| Figure of merit before/after density modification | 0.34/0.58 | ||
| Structure refinement | |||
| Resolution | 50–1.70 | 50–1.85 | 50–2.04 |
| Rwork/Rfree, %§ | 16.9/19.8 | 17.9/21.5 | 19.3/24.3 |
| Protein/solvent atoms | 568/103 | 572/53 | 1701/90 |
| Bond length deviation from ideal geometry (Å) | 0.006 | 0.006 | 0.007 |
| Bond angle deviation from ideal geometry (°) | 0.986 | 1.0646 | 1.040 |
| Ramachandran favored/allowed/outliers (%) | 98.6/1.4/0 | 100/0/0 | 98.6/1.4/0 |
| Average B factor for protein/solvent | 22.0/33.8 | 34.9/39.3 | 32.9/33.8 |
*Experimental data has been deposited with the indicated deposition ID codes.
†Values in parentheses are for highest-resolution shell.
‡
where I(i, h) and <I(h)> are the ith and mean measurement of intensity of reflection h.
§The Rfree value was calculated using 5% of the data.