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 |