Table I. Data collection, structure determination and refinement statistics.
Data collection and MIR phasing statistics | |||||||
Data set | Resolution (Å) | Observations/unique reflections | Completeness (last shell) % | Rmergea (last shell) | |||
SeMet λ1 | 3.2 | 78580/60509 | 88.9 (84.1) | 0.047 (0.15) | |||
SeMet λ2 | 3.2 | 86114/63424 | 92.8 (85.4) | 0.066 (0.25) | |||
Native |
2.6 |
259515/71198 |
99.3 (99.2) |
0.084 (0.28) |
|
|
|
Structure refinement statistics | |||||||
Resolution (Å) | Protein atoms | Waters | Rcrystb | Rfreeb (% data used) | R.m.s.d. from idealityc | ||
Bonds | Angles | Dihedrals | |||||
25.0–2.6 | 9551 | 121 | 26.46 | 29.43 (3) | 0.0072 | 1.3921 | 24.76 |
aRmerge = ΣhklΣi|Ii(hkl) – <I(hkl)>|/ΣhklΣi Ii(hkl).
bRcryst and Rfree = Σ|Fobs – Fcalc|/ΣFobs; Rfree calculated with the percentage of the data shown in parentheses.
cR.m.s.ds for bond angles and lengths in regard to Engh and Huber parameters.