6JU5
Aspergillus oryzae pro-tyrosinase C92A/F513Y mutant
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 | CCD |
| Collection date | 2016-11-24 |
| Detector | RAYONIX MX300HE |
| Wavelength(s) | 0.900 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 54.344, 118.210, 79.363 |
| Unit cell angles | 90.00, 91.13, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.340 |
| R-factor | 0.1593 |
| Rwork | 0.157 |
| R-free | 0.20220 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3w6w |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.020 |
| Data reduction software | DENZO |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | SHELXL (2017/1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.360 |
| High resolution limit [Å] | 1.340 | 1.340 |
| Rmerge | 0.076 | 0.690 |
| Number of reflections | 223551 | 11171 |
| <I/σ(I)> | 17.3 | 2.1 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 3.8 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.2 | 293 | 19% polyethylene glycol (PEG) 3350, 30mM NH4NO3 |






