1L76
TOLERANCE OF T4 LYSOZYME TO PROLINE SUBSTITUTIONS WITHIN THE LONG INTERDOMAIN ALPHA-HELIX ILLUSTRATES THE ADAPTABILITY OF PROTEINS TO POTENTIALLY DESTABILIZING LESIONS
Experimental procedure
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 60.770, 60.770, 98.620 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 1.900 |
| R-factor | 0.167 |
| RMSD bond length | 0.013 |
| RMSD bond angle | 2.000 |
| Refinement software | TNT |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 1.900 * |
| Rmerge | 0.055 * |
| Number of reflections | 15147 * |
| Completeness [%] | 89.4 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Batch method * | Remington, S.J., (1978) J. Mol. Biol., 118, 81. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | protein | 20 (mg/ml) | |
| 2 | 1 | 1 | 0.55 (M) | ||
| 3 | 1 | 1 | mercaptoethanol | 14 (mM) | |
| 4 | 1 | 1 | 1 (mM) | ||
| 5 | 1 | 1 | sodium phospahte | 0.01 (M) | |
| 6 | 1 | 1 | 2.2 (M) | ||
| 7 | 1 | 1 | 1.8 (M) |
