177L
Protein flexibility and adaptability seen in 25 crystal forms of T4 LYSOZYME
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 290 |
| Detector technology | AREA DETECTOR |
| Collection date | 1993-12-29 |
| Detector | XUONG-HAMLIN MULTIWIRE |
| Spacegroup name | P 42 2 2 |
| Unit cell lengths | 72.600, 72.600, 82.200 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.500 |
| R-factor | 0.228 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.015 |
| RMSD bond angle | 2.400 |
| Data reduction software | Xuong-Hamlin |
| Data scaling software | Rotovata/Agrovata |
| Phasing software | MRX |
| Refinement software | TNT |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 20.000 |
| High resolution limit [Å] | 2.500 |
| Number of reflections | 7778 |
| Completeness [%] | 97.0 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8.6 | pH 8.6 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | ammonium sulfate | 1.8 (M) | |
| 2 | 1 | reservoir | 0.1 (M) | ||
| 3 | 1 | reservoir | Tris-HCl | 0.1 (M) | |
| 4 | 1 | reservoir | reduced beta-mercaptoethanol | 50 (mM) |






