From: Conformational changes and loose packing promote E. coli Tryptophanase cold lability
Y74F [PDB:2V1P] | C298S [pdb:2V0Y] | |
---|---|---|
Data collection | ||
Space group | F222 | F222 |
Wavelength | 1.5Å | 1.5Å |
Unit cell | a = 118.7Å | a = 120.5Å |
b = 120.2Å | b = 118.8Å | |
c = 171.7Å | c = 171.5Å | |
α = 90° | α = 90° | |
β = 90° | β = 90° | |
γ = 90° | γ = 90° | |
Resolution | 500.0-1.90 Å | 500.0-1.98 Å |
Highest resolution shell | 1.97-1.90 Å | 2. 05-1.98 Å |
Total number of measured reflections Total number of independent reflections |
155,699 47,181 |
186,657 42,496 |
Completeness (%) | 97.6% (97.8%) | 99.3% (96.5%) |
Rsym | 0.054 (0.410) | 0.117 (0.456) |
I/σ (I) | 19.0 (2.9) | 12.7 (2.9) |
Refinement | ||
Resolution range (Å) | 6.0-1.9 | 8.0-2.0 |
R (%) | 19.14 | 21.48 |
Rfree (%) | 22.72 | 22.09 |
Protein atoms | 3682 | 3678 |
Solvent atoms | 595 | 519 |
Mg2+ atoms | 1 | 1 |
Cl- atoms | 1 | 1 |
RMS deviations from restraints target value | ||
Bond length (Å) | 0.005 | 0.006 |
Bond Angle (°) | 1.21 | 1.22 |
Average B factor (for protein atoms) (Å2) | 28.8 | 28.9 |