Table 1.
Data collection, phasing and refinement statistics
| Free | ADDATRX–H31–15 | ADDATRX–H31–15K9me3 | ||
|---|---|---|---|---|
| Data Collection | Zn-SAD | Native | Native | Native |
| Space group | P32 | P3221 | P65 | C2 |
| Cell dimensions | ||||
| a, b, c (Å) | 74.2, 74.2, 54.1 | 80.6, 80.6, 136.1 | 66.7, 66.7, 131.6 | 83.7, 39.5, 41.1 |
| α, β, γ (°) | 90, 90, 120 | 90, 90, 120 | 90, 90, 120 | 90, 111.2, 90 |
| Peak | ||||
| Wavelength (Å) | 1.2827 | 0.9795 | 0.9792 | 0.9792 |
| Resolution (Å) | 50–1.9 (1.93–1.90)* | 50–2.5 (2.56–2.50) | 50–1.6 (1.63–1.60) | 50–0.93 (0.95–0.93) |
| Rsym (%) | 6.3 (55.4) | 6.3 (53.2) | 8.3 (56.6) | 6.7 (57.0) |
| I/σI | 43.6 (4.0) | 40.4 (4.0) | 23.3 (2.7) | 35.5 (3.5) |
| Completeness (%) | 99.9 (100.0) | 99.7 (100.0) | 98.5 (97.3) | 93.1 (88.1) |
| Redundancy | 5.6 (5.5) | 12.4 (7.7) | 9.7 (9.3) | 8.5 (8.2) |
| Refinement (F>0) | ||||
| No. reflections (overall) | 26159 | 18264 | 41649 | 76594 |
| No. refelctions (test set) | 1997 | 1473 | 2093 | 3831 |
| Twinning fraction | 0.408 | |||
| Rwork/Rfree (%) | 12.7/15.8 | 19.4/24.1 | 15.7/17.9 | 12.2/13.1 |
| No. non–H atoms | ||||
| Protein | 1935 | 2016 | 1976 | 1085 |
| Ligand/ion | –/6 | 106/6 | 176/6 | 93/3 |
| Water | 334 | 114 | 471 | 240 |
| B-factors (Å2) | ||||
| Protein | 35.5 | 51.1 | 18.6 | 8.1 |
| Ligand/ion | –/37.0 | 60.7 | 21.6/12.1 | 12.9/3.8 |
| Water | 38.0 | 45.5 | 31.5 | 14.0 |
| R.m.s. deviations | ||||
| Bond lengths (Å) | 0.006 | 0.009 | 0.015 | 0.020 |
| Bond angles (°) | 0.92 | 1.13 | 1.37 | 1.41 |
*
Each data set was collected from a single crystal; values in parentheses are for highest resolution shell.