TABLE 1.
Data collection | Valuea |
|
---|---|---|
Monoclinic | Orthorhombic | |
Space group | P21 | C2221 |
Unit cell a, b, c (Å) | 57.75, 86.26, 83.51 | 86.26, 105.22, 84.05 |
Unit cell α, β, γ (Å) | 90.0, 110.95, 90.0 | 90.0, 90.0, 90.0 |
Wavelength (Å) | 0.97872 | 0.97856 |
Resolution (Å) | 2.0 (2.03-2.0) | 2.0 (2.07-2.00) |
Rsym (%)b | 7.8 (37) | 7.1 (27) |
<I/sI>c | 10 (2) | 10 (10) |
Completeness (%)d | 99.4 (93.3) | 93.3 (68.1) |
Redundancy | 3.7 (2.8) | 4.4 (3.5) |
Refinement | ||
Resolution (Å) | 2.0 | 2.0 |
R factor (%)e | 17.87 | 19.06 |
Rfree (%)f | 23.18 | 25.64 |
No. of protein atoms | 5,307 | 2,676 |
No. of water molecules | 650 | 304 |
No. of unique reflections | 48,795 | 24,409 |
Rmsdg | ||
Bonds | 0.017 | 0.026 |
Angles | 1.898 | 2.139 |
Statistics for the highest-resolution bin of reflections are in parentheses.
Rsym = ΣhΣj l Ihj − <Ih> l/ΣhΣjIhj, where Ihj is the intensity of observation j of reflection h and <Ih> is the mean intensity for multiply recorded reflections.
Intensity signal-to-noise ratio.
Completeness of the unique diffraction data.
R factor = Σh I IFoI − IFcI I/ΣhIFoI, where Fo and Fc are the observed and calculated structure factor amplitudes for reflection h.
Rfree was calculated against a 10% random sampling of the reflections that were removed before structure refinement.
RMSD of bond lengths and bond angles.