Table 1.
Data Collection and Refinement Statistics for the pII-MarVIF Crystal Structure
| pII-MarVIF | |
|---|---|
| PDB entry | 4G2K |
| Data Collection | |
| Wavelength (Å) | 1.075 |
| Space group | P21 21 2 |
| Unit cell dimensions (Å) | a = 52.57 |
| b = 147.53 | |
| c = 42.20 | |
| α = β = γ = 90° | |
| Resolution range (Å) | 1.9 – 20.0 |
| Observed reflections | 260,604 |
| Unique reflections | 26,888 |
| Completeness (%) a | 99.6(94.3) |
| Rsym | 0.071(0.583) |
| I/σI | 11.5(2.9) |
| R-merge (I) b | |
| Structure Refinement | |
| Rcryst (%) c | 0.197 |
| Rfree (%) c | 0.248 |
| Protein nonhydrogen atoms | 2421 |
| Water molecules | 249 |
| Average B-factor (Å2) | 35.0 |
| RMS Deviations from Ideal Value | |
| Bonds (Å) | 0.011 |
| Angles (°) | 1.28 |
| Torsion angles (°) | 17.1 |
a
Values in parentheses indicate statistics for the high resolution bin (1.95 – 1.9 Å)
b
Rmerge = ΣΣ j|Ij(hkl) – <I(hkl)>|/ ΣΣ j|<I(hkl)>|, where Ij is the intensity measurement for reflection j and <I> is the mean intensity over j reflections.
c
Rcryst/(Rfree) = Σ ‖|Fo(hkl)| – |Fc(hkl)‖/ Σ |Fo(hkl)|, where Fo and Fc are observed and calculated structure factors, respectively. No σ-cutoff was applied. 5% of the reflections were excluded from refinement and used to calculate Rfree.