Table 3. Data collection, structure solution, and initial model building statistics resulting from I-SAD/I-SIRAS phasing of the crystal structure of KR2 using diffraction data collected using serial methods.
| I-SAD | I-SIRAS | I-SAD | I-SIRAS | |||||
| Data collection |
No. of crystals | 136 | 39 | Structure solution and Refinement |
Initial resolution range (Å) |
60–2.8 | 60–2.9 | |
| Method | SAD | SIRAS | Number of residues in the protein |
288 | 288 | |||
| Space group | I222 | I222 | Substructure | 16·I | 12·I | |||
| Unit cell | a | 40.6 | 41.0 | Resolution cutoff for substructure search (Å) |
3.9 | 3.4 | ||
| b | 83.6 | 84.0 | Resolution extension by native data (Å) |
2.5 | 2.5 | |||
| c | 233.5 | 234.3 | CCall/CCweak | 38.7/11.0 | 26.7/9.6 | |||
| No. of frames | 13,600 | 3900 | Solvent content (%) |
63 | 60 | |||
| Oscillation range (°) |
0.1 | 0.1 | CCmap, highest-resolution shell (%) |
47 | 67 | |||
| Resolution range (Å) |
60–2.8 (3.0–2.8) | 60–2.9 (3.1–2.9) | Number of Ala residues traced by SHELXE |
122 | 165 | |||
| Measured reflections |
469,213 (85,461) | 124,613 (22,610) |
Rwork/Rfree after initial model building (%) |
29.6/35.7† | 24.2/31.6* 29.9/35.4† |
|||
| Multiplicity | 24.79 (24.13) | 7.19 (7.13) | Number of residues built in initial model building |
207† | 248* 196† |
|||
| Completeness (%) | 100 (100) | 99.8 (100) | ||||||
| Rmerge (%) | 61.7 (220.7) | 23.8 (154.6) | ||||||
| Rmeas (%) | 63.0 (225.4) | 25.6 (166.6) | ||||||
| <I/σ(I)> | 10.64 (2.27) | 7.71 (1.69) | ||||||
| CC1/2 (%) | 99.8 (70.1) | 99.3 (56.2) | ||||||
| SigAno | 1.21 (0.78) | 1.03 (0.73) | ||||||
| CCanom (%) | 39 (0) | 29 (−1) |
*Model built by ARP-wARP.
†Model built by phenix.autobuild.