Table 1.
Crystallographic data collection, structure solution, and refinement
| Crystal [space group] | λ (Å) | d (mi) (Å) | No. data | Completeness (%) | Multiplicity | I/σ (last shell) | Rsymb (%) | Phasing powerc iso/ano | Rcullisd iso/ano |
|---|---|---|---|---|---|---|---|---|---|
| X-ray data collection | |||||||||
| P/H:F23ta [P3121] | 0.8460 | 2.6 | 16,619 | 98.3 | 5.2 | 21.8 (2.5) | 4.7 (35.0) | — | — |
| P/H:F22ta (br)-peak [P6422] | 0.9198 | 3.0 | 24,450a | 99.6 | 5.5 | 17.0 (2.4) | 4.3 (53.2) | —/1.63 | —/0.79 |
| P/H:F22ta (br)-infl. | 0.9202 | 3.0 | 24,366a | 99.5 | 4.3 | 19.2 (2.0) | 3.9 (55.1) | 3.02/1.08 | 0.47/0.92 |
| P/H:F22ta (br)-high | 0.9068 | 3.0 | 22,662a | 92.2 | 2.9 | 15.1 (1.7) | 4.5 (56.8) | 0.98/2.05 | 0.61/0.82 |
| Crystal | Resolution (Å) | Protein atoms | DNA atoms | Solvent atoms | RMSd bond length (Å) | RMSd bond angles (°) | Rcryste (%) | Rfreee (%) | <B> (Å2) protein/DNA |
| Structure refinement | |||||||||
| P/H:F23ta | 30.0-2.6 | 1765 | 978 | 90 | 0.010 | 1.8 | 23.2 | 28.5 | 61/54 |
a
Friedel mates were not merged during scaling.
b
Rsym = ΣhklΣi|Ii (hkl) - <I(hkl)>|/ΣhklΣI Ii(hkl).
c
Phasing power is defined as the ratio of the RMS value of the heavy atom structure factor amplitudes and the RMS value of the lack-of closure error.
d
Rcullis is the mean lack-of-closure error divided by the isomorphous/anomalous difference.
e
Rcryst and Rfree = |ΣFobs - Fcalc|/ΣFobs; Rfree is calculated with 5% of the data that were not used for refinement.