8IUW
Crystal structure of Copper-bound N(omega)-hydroxy-L-arginine hydrolase with oxidized Cys86
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL44XU |
| Synchrotron site | SPring-8 |
| Beamline | BL44XU |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2020-02-14 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.35 |
| Spacegroup name | P 1 |
| Unit cell lengths | 46.400, 47.145, 59.393 |
| Unit cell angles | 83.69, 84.70, 70.27 |
Refinement procedure
| Resolution | 44.220 - 1.500 |
| R-factor | 0.1701 |
| Rwork | 0.168 |
| R-free | 0.20410 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.856 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((1.17.1_3660: 000)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 44.220 | 1.530 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.050 | 0.704 |
| Rmeas | 0.059 | 0.824 |
| Rpim | 0.031 | 0.426 |
| Total number of observations | 256067 | 11971 |
| Number of reflections | 70228 | 3255 |
| <I/σ(I)> | 13.7 | 1.9 |
| Completeness [%] | 93.3 | |
| Redundancy | 3.6 | 3.7 |
| CC(1/2) | 0.998 | 0.708 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.3 | 298 | PEG 4000, MgCl2 |
