1L35
STRUCTURE OF A THERMOSTABLE DISULFIDE-BRIDGE MUTANT OF PHAGE T4 LYSOZYME SHOWS THAT AN ENGINEERED CROSSLINK IN A FLEXIBLE REGION DOES NOT INCREASE THE RIGIDITY OF THE FOLDED PROTEIN
Experimental procedure
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 61.200, 61.200, 96.900 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 6.000 - 1.800 |
| R-factor | 0.157 |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.980 |
| Refinement software | TNT |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 1.800 * |
| Rmerge | 0.069 * |
| Number of reflections | 14686 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Batch method * | 6.5 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | protein | 15 (mg/ml) | |
| 2 | 1 | 1 | 0.1 (M) | ||
| 3 | 1 | 1 | 0.55 (M) | ||
| 4 | 1 | 1 | 0.02 (%) | ||
| 5 | 1 | 1 | 4 (M) | ||
| 6 | 1 | 1 | 2-mercaptoethanol | 10 (mM) |
