1B2R
FERREDOXIN-NADP+ REDUCTASE (MUTATION: E 301 A)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM02 |
| Synchrotron site | ESRF |
| Beamline | BM02 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1998-02-15 |
| Spacegroup name | P 65 |
| Unit cell lengths | 86.650, 86.650, 96.260 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 7.000 - 1.800 |
| R-factor | 0.19 * |
| Rwork | 0.190 |
| R-free | 0.24000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1que |
| RMSD bond length | 0.008 |
| RMSD bond angle | 26.660 * |
| 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] | 37.500 | 1.930 |
| High resolution limit [Å] | 1.800 | 1.810 |
| Rmerge | 0.067 | 0.072 |
| Number of reflections | 38021 | |
| <I/σ(I)> | 8.1 | 10.3 |
| Completeness [%] | 98.6 | 91.8 |
| Redundancy | 5.2 | 2.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8 * | 20 * | 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. |
| 3 | 1 | drop | beta-octylglucoside | 5 (%(w/v)) | |
| 4 | 1 | reservoir | PEG6000 | 17 (%(w/v)) | |
| 5 | 1 | reservoir | ammonium sulfate | 20 (mM) | |
| 6 | 1 | reservoir | MES- NaOH | 0.1 (M) | pH5.0 |
