Table 2 Crystallization conditions, data collection, and refinement statistics
Amino acid residue boundaries | 696–1022 |
|---|---|
PBD ID | 7TVD |
Crystallization conditions | Protein in 20 mM Tris pH 8.0, 150 mM NaCl and 2% glycerol: Reservoir solution 28% PEG 400, 0.1 M HEPES pH 7.5, 0.2 M CaCl2. Ratio = 1:1, 16 °C |
Data collectiona | |
   Beamline | APS/NE-CAT 24-ID-C |
   Date of collection | March 19, 2019 |
   Wavelength (Å) | 0.97918 |
   Space group | I 2 3 |
Cell dimensions | |
   a, b, c (Å) | 149.42, 149.42, 149.42 |
   α, β, γ (°) | 90.00, 90.00, 90.00 |
   Resolution (Å) | 105.66–2.96 |
   Completeness | 99.9 (99.7) |
   Redundancy | 36.1 (33.5) |
   Rsym (%) | 44 (263) |
   I/σ | 15.4 (1.5) |
   CC1/2 | 0.999 (0.44) |
 Number of reflections | 11,749 (1880) |
Refinement | |
   Rwork/Rfree (%) | 24.0/27.7 |
Number of atoms | |
   Protein | 2338 |
   Ions | 0 |
   Ligands | 0 |
   Water | 0 |
Average B factor (Ã…) | |
   Protein | 104.0 |
   Ions | - |
   Ligands | - |
   Water | - |
Geometry (Ramachandran) | |
   Favored (%) | 94.06 |
   Allowed (%) | 5.24 |
   Outliers (%) | 0.70 |
RMSD (Ã…) | |
   Bond length | 0.004 |
   Bond angle | 0.77 |
