1GR1
Structure of Ferredoxin-NADP+ Reductase with Glu 139 replaced by Lys (E139K)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | ENRAF-NONIUS FR571 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2001-06-15 |
| Detector | MARRESEARCH |
| Spacegroup name | P 65 |
| Unit cell lengths | 87.030, 87.030, 96.370 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 10.000 - 2.500 |
| R-factor | 0.18 |
| Rwork | 0.180 |
| R-free | 0.25000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1que |
| RMSD bond length | 0.008 |
| RMSD bond angle | 26.591 * |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | X-PLOR (3.843) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 27.300 | 2.640 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.167 | 0.264 |
| Number of reflections | 13944 | |
| <I/σ(I)> | 3.2 | 2.6 |
| Completeness [%] | 97.1 | 99.9 |
| Redundancy | 3.9 | 4.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8 * | 20-23 * | pH 5.50 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 0.75 (mM) | |
| 2 | 1 | drop | Tris-HCl | 10 (mM) | pH8.0 |
| 3 | 1 | reservoir | beta-octylglucoside | 5 (%(w/v)) | |
| 4 | 1 | reservoir | PEG6000 | 18 (%) | |
| 5 | 1 | reservoir | ammonium sulfate | 20 (mM) | |
| 6 | 1 | reservoir | MES- NaOH | 0.1 (M) | pH5.5 |
