212L
PROTEIN STRUCTURE PLASTICITY EXEMPLIFIED BY INSERTION AND DELETION MUTANTS IN T4 LYSOZYME
Experimental procedure
| Detector technology | AREA DETECTOR |
| Collection date | 1994-11-02 |
| Detector | XUONG-HAMLIN MULTIWIRE |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 60.910, 60.910, 96.730 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 35.650 - 1.760 |
| R-factor | 0.156 * |
| Rwork | 0.156 |
| RMSD bond length | 0.013 |
| RMSD bond angle | 2.000 |
| Data reduction software | UCSD |
| Refinement software | TNT |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 35.650 |
| High resolution limit [Å] | 1.760 |
| Rmerge | 0.062 |
| Number of reflections | 20392 |
| Completeness [%] | 95.3 |
| Redundancy | 2.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | unknown * | 7.5 * | MUTANT CRYSTALLIZED FROM PEG IN CONTRAST TO L164AAAA WHICH WAS CRYSTALLIZED FROM PHOSPHATE. |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | PEG8000 | 18 (%) | |
| 2 | 1 | 1 | HEPES | 0.1 (M) | |
| 3 | 1 | 1 | beta-mercaptoethanol | 50 (mM) |
