1L41
CONTRIBUTIONS OF ENGINEERED SURFACE SALT BRIDGES TO THE STABILITY OF T4 LYSOZYME DETERMINED BY DIRECTED MUTAGENESIS
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | ELLIOTT GX-21 |
| Temperature [K] | 298 |
| Detector technology | FILM |
| Detector | OSCILLATION CAMERA |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 60.600, 60.600, 96.900 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 6.000 - 1.750 |
| R-factor | 0.157 |
| RMSD bond length | 0.018 |
| RMSD bond angle | 0.016 * |
| Data scaling software | AGROVATA / ROTAVATA |
| Refinement software | TNT |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 1.750 * |
| Rmerge | 0.068 * |
| Number of reflections | 14683 * |
| Completeness [%] | 68.0 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Batch method * | taken from Remington, S.J. et al (1978). J. Mol. Biol., 81-98. * |
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) |
