1BQE
FERREDOXIN:NADP+ REDUCTASE MUTANT WITH THR 155 REPLACED BY GLY (T155G)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | ENRAF-NONIUS FR571 |
| Temperature [K] | 291 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-02 |
| Detector | MAR scanner 180 mm plate |
| Spacegroup name | P 65 |
| Unit cell lengths | 88.130, 88.130, 97.250 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 9.000 - 2.400 * |
| R-factor | 0.16 |
| Rwork | 0.160 |
| R-free | 0.24000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1que |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.400 |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | AMoRE |
| Refinement software | X-PLOR (3.843) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.100 * | 2.580 |
| High resolution limit [Å] | 2.400 * | 2.450 |
| Rmerge | 0.100 * | 0.270 |
| Number of reflections | 15728 | |
| <I/σ(I)> | 6.3 | 2.7 |
| Completeness [%] | 99.5 | 97.2 * |
| Redundancy | 7.7 | 6.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8 * | pH 5.0 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 25.9 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 10 (mM) | pH8.0 |
| 3 | 1 | drop | beta-octylglucoside | 5 (%(w/v)) | |
| 4 | 1 | reservoir | PEG6000 | 18 (%(w/v)) | |
| 5 | 1 | reservoir | ammonium sulfate | 20 (mM) | |
| 6 | 1 | reservoir | sodium acetate | 0.1 (M) | pH5.0 |
