4C43
FERREDOXIN NADP REDUCTASE MUTANT WITH GLU 103 REPLACED BY TYR, TYR 104 REPLACED BY PHE, SER 109 REPLACED BY PHE AND GLY 110 REPLACED BY PRO (E103Y-Y104F-S109F-G110P)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | ADSC QUANTUM 315r |
| Spacegroup name | P 65 |
| Unit cell lengths | 87.410, 87.410, 96.448 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 43.710 - 1.700 |
| R-factor | 0.17698 |
| Rwork | 0.175 |
| R-free | 0.20496 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1que |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.293 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 43.710 | 1.790 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.080 | 0.270 |
| Number of reflections | 45911 | |
| <I/σ(I)> | 16.1 | 5.7 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 9.3 | 9.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 18-20% PEG 6000,20 MM AMMONIUM SULFATE, 0.1 M MES/NAOH, PH 5.0. |
