8I99
N-carbamoyl-D-amino-acid hydrolase mutant - M4Th3
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SEALED TUBE |
| Source details | BRUKER D8 QUEST |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2022-11-22 |
| Detector | Bruker PHOTON II |
| Wavelength(s) | 1.54178 |
| Spacegroup name | P 1 |
| Unit cell lengths | 71.143, 73.548, 77.711 |
| Unit cell angles | 84.08, 88.20, 89.73 |
Refinement procedure
| Resolution | 23.980 - 3.170 |
| R-factor | 0.2047 |
| Rwork | 0.201 |
| R-free | 0.27750 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.291 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | PHENIX (v1.20) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 23.980 | 3.390 |
| High resolution limit [Å] | 3.170 | 3.170 |
| Rmerge | 0.128 | 0.307 |
| Number of reflections | 26181 | 4578 |
| <I/σ(I)> | 4 | |
| Completeness [%] | 98.7 | |
| Redundancy | 1.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 285 | Bis-Tris pH6.5, PEG 3350 |
