3C8R
Contributions of all 20 amino acids at site 96 to stability and structure of T4 lysozyme
Replaces: 2NZKExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 298 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-06-01 |
| Detector | RIGAKU |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 61.090, 61.090, 97.840 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.500 - 1.800 |
| R-factor | 0.172 |
| Rwork | 0.172 |
| R-free | 0.17200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1l63 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.144 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | TNT |
| Refinement software | TNT |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.500 | 1.900 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.067 | 0.322 |
| Number of reflections | 18258 | |
| <I/σ(I)> | 21.8 | 4.5 |
| Completeness [%] | 92.2 | 96.2 |
| Redundancy | 5 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.7 | 2M NA/K PHOSPHATE 50 MM REDUCED BME 50 MM OXIDIZED BME, PH 6.7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 276K, PH 6.70 |
