Crystallographic statistics
| . | α0-1/β16-17 . |
|---|---|
| Data collection | |
| Detector type/source | MarCCD (Rayonix)/Advanced Photo Source |
| Wavelength, Å | 0.97872 |
| Resolution,* Å | 40.0-2.80 (2.92-2.80) |
| Measured reflections | 54 695 (6817) |
| Unique reflections | 18 015 (2195) |
| Completeness | 98.6 (99.3) |
| Multiplicity | 3.0 (3.1) |
| Mean [I/σ(I)] | 13.5 (3.4) |
| Rsym, %† | 5.7 (29.7) |
| Rmeas,%‡ | 7.0 (35.8) |
| Refinement | |
| Resolution | 35.0-2.80 (2.87-2.80) |
| Number of reflections working/test | 17 085/922 (1251/76) |
| R-work, %§ | 26.8 (40.9) |
| R-free, %‖ | 29.9 (40.5) |
| Protein atoms | 2673 |
| Bond lengths | 0.011 |
| Bond angles | 1.24 |
| . | α0-1/β16-17 . |
|---|---|
| Data collection | |
| Detector type/source | MarCCD (Rayonix)/Advanced Photo Source |
| Wavelength, Å | 0.97872 |
| Resolution,* Å | 40.0-2.80 (2.92-2.80) |
| Measured reflections | 54 695 (6817) |
| Unique reflections | 18 015 (2195) |
| Completeness | 98.6 (99.3) |
| Multiplicity | 3.0 (3.1) |
| Mean [I/σ(I)] | 13.5 (3.4) |
| Rsym, %† | 5.7 (29.7) |
| Rmeas,%‡ | 7.0 (35.8) |
| Refinement | |
| Resolution | 35.0-2.80 (2.87-2.80) |
| Number of reflections working/test | 17 085/922 (1251/76) |
| R-work, %§ | 26.8 (40.9) |
| R-free, %‖ | 29.9 (40.5) |
| Protein atoms | 2673 |
| Bond lengths | 0.011 |
| Bond angles | 1.24 |
Numbers in parentheses correspond to the highest-resolution shell throughout.
Rsym = Σ I−<I> /ΣI, where I is the observed intensity and <I> the average intensity obtained from multiple measurements.
Rmeas as described in Diederichs and Karplus.29
R-work=Σ Fo − Fc /Σ Fo, where Fo is the observed structure factor amplitude and Fc the calculated structure factor amplitude.
Rfree: R-factor determined on the basis of 5% of the data excluded from refinement.