3A9Z
Crystal structure of ras selenocysteine lyase in complex with selenopropionate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL32B2 |
| Synchrotron site | SPring-8 |
| Beamline | BL32B2 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 55.416, 101.206, 197.356 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.990 - 1.550 |
| R-factor | 0.187 |
| Rwork | 0.187 |
| R-free | 0.20900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.029 |
| RMSD bond angle | 2.400 |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.610 |
| High resolution limit [Å] | 1.550 | 1.550 |
| Number of reflections | 159678 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.7 | 293 | 1.5M ammonium dihydrogen phosphate, pH 4.7, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
