5JCN
Structure and catalytic mechanism of monodehydroascorbate reductase, MDHAR, from Oryza sativa L. japonica
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 | 2015-06-18 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 0.9000 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 79.635, 85.112, 133.443 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.290 |
| R-factor | 0.2082 |
| Rwork | 0.205 |
| R-free | 0.26360 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4h4q |
| RMSD bond length | 0.015 |
| RMSD bond angle | 2.038 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0103) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 71.760 | 50.000 | 2.340 |
| High resolution limit [Å] | 2.290 | 6.240 | 2.300 |
| Rmerge | 0.087 | 0.061 | |
| Rmeas | 0.089 | 0.064 | |
| Rpim | 0.029 | 0.020 | 0.502 |
| Total number of observations | 571023 | ||
| Number of reflections | 41172 | ||
| <I/σ(I)> | 13 | ||
| Completeness [%] | 99.5 | 92.2 | 100 |
| Redundancy | 13.9 | 9.9 | 14.9 |
| CC(1/2) | 0.997 | 0.699 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 295 | Tris, ammonium acetate, PEG 3350 |
