PROTEIN ENGINEERING OF XYLOSE (GLUCOSE) ISOMERASE FROM ACTINOPLANES MISSOURIENSIS. 1. CRYSTALLOGRAPHY AND SITE-DIRECTED MUTAGENESIS OF METAL BINDING SITES
X-RAY DIFFRACTION
Crystallization
| Crystal Properties | |
|---|---|
| Matthews coefficient | Solvent content |
| 3.96 | 68.92 |
Crystal Data
| Unit Cell | |
|---|---|
| Length ( Å ) | Angle ( ˚ ) |
| a = 143.45 | α = 90 |
| b = 143.45 | β = 90 |
| c = 231.5 | γ = 120 |
| Symmetry | |
|---|---|
| Space Group | P 32 2 1 |
Refinement
| Statistics | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Diffraction ID | Structure Solution Method | Resolution (High) | Resolution (Low) | Number Reflections (Observed) | Number Reflections (R-Free) | Percent Reflections (Observed) | R-Factor (Observed) | R-Work (Depositor) | R-Free (Depositor) | Mean Isotropic B | |||||||||
| X-RAY DIFFRACTION | 2.6 | 71972 | 0.144 | ||||||||||||||||
| RMS Deviations | |
|---|---|
| Key | Refinement Restraint Deviation |
| p_multtor_nbd | 0.266 |
| p_chiral_restr | 0.135 |
| p_angle_d | 0.042 |
| p_planar_d | 0.04 |
| p_bond_d | 0.013 |
| p_plane_restr | 0.01 |
| p_angle_deg | |
| p_hb_or_metal_coord | |
| p_mcbond_it | |
| p_mcangle_it | |
| Non-Hydrogen Atoms Used in Refinement | |
|---|---|
| Non-Hydrogen Atoms | Number |
| Protein Atoms | 12212 |
| Nucleic Acid Atoms | |
| Solvent Atoms | 868 |
| Heterogen Atoms | 52 |
Software
| Software | |
|---|---|
| Software Name | Purpose |
| PROLSQ | refinement |
