1MYL
SUBSTITUTING HYDROPHOBIC RESIDUES FOR A BURIED SALT BRIDGE ENHANCES PROTEIN STABILITY BUT DOES NOT REDUCE CONFORMATIONAL SPECIFICITY
Experimental procedure
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 29.600, 117.100, 49.700 |
| Unit cell angles | 90.00, 98.60, 90.00 |
Refinement procedure
| Resolution | 6.000 - 2.400 |
| R-factor | 0.209 |
| Rwork | 0.209 |
| R-free | 0.29300 |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.550 |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 2.400 * |
| Rmerge | 0.062 * |
| Total number of observations | 20111 * |
| Number of reflections | 11168 |
| Completeness [%] | 90.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | protein | 15 (mg/ml) | |
| 2 | 1 | 1 | bis-Tris-propane-Cl | 30 (mM) | |
| 3 | 1 | 1 | 1 (mM) | ||
| 4 | 1 | 2 | PEG3400 | 19-22 (%) | |
| 5 | 1 | 2 | Tris-HCl | 100 (mM) | |
| 6 | 1 | 2 | Na-acetate | 200 (mM) |






