2VYQ
FERREDOXIN:NADP REDUCTASE MUTANT WITH THR 155 REPLACED BY GLY, ALA 160 REPLACED BY THR, LEU 263 REPLACED BY PRO AND TYR 303 REPLACED BY SER (T155G-A160T-L263P-Y303S)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | BRUKER AXS MICROSTAR |
| Temperature [K] | 120 |
| Detector technology | CCD |
| Collection date | 2006-06-30 |
| Detector | BRUKER-NONIUS |
| Spacegroup name | P 65 |
| Unit cell lengths | 87.021, 87.021, 96.106 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 19.800 - 1.900 |
| R-factor | 0.163 |
| Rwork | 0.161 |
| R-free | 0.18500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1que |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.023 |
| Data reduction software | SAINT (2006) |
| Data scaling software | SADABS (2006) |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 75.380 | 2.000 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.050 | 0.190 |
| Number of reflections | 30845 | |
| <I/σ(I)> | 23.85 | 5.45 |
| Completeness [%] | 99.1 | 93.8 |
| Redundancy | 5.26 | 2.54 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.5 | 18-20 % (W/V) PEG 6000 20 MM AMMONIUM SULPHATE 0.1M MES/NAOH, PH 5.0-5.5 B-OCTYL GLYCOSIDE AT 2%(W/V) |
