2V0Y
Crystal structure of apo C298S tryptophanase from E.coli
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Detector | RIGAKU RAXIS IV |
| Spacegroup name | F 2 2 2 |
| Unit cell lengths | 120.484, 118.770, 171.534 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 80.000 - 2.000 |
| R-factor | 0.2148 |
| Rwork | 0.215 |
| R-free | 0.25690 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2oqx |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.000 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 500.000 | 2.050 |
| High resolution limit [Å] | 1.980 | 1.980 |
| Rmerge | 0.120 | 0.460 |
| Number of reflections | 42496 | |
| <I/σ(I)> | 12.7 | |
| Completeness [%] | 99.3 | 96.5 |
| Redundancy | 4.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | PEG 400 30% V/W, HEPES 100 MM, PH 7.5 MGCL2 200MM |
