1MRZ
Crystal structure of a flavin binding protein from Thermotoga Maritima, TM379
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.2 |
| Synchrotron site | ALS |
| Beamline | 5.0.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2001-05-02 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.97911 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 67.211, 83.095, 67.851 |
| Unit cell angles | 90.00, 116.93, 90.00 |
Refinement procedure
| Resolution | 30.000 * - 1.900 |
| R-factor | 0.21696 |
| Rwork | 0.217 |
| R-free | 0.23300 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | MAD |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.120 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | REFMAC (5.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 * | 1.930 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.038 * | 0.299 * |
| Number of reflections | 51627 * | 2190 * |
| <I/σ(I)> | 27 | 4.1 |
| Completeness [%] | 96.9 | 82.2 |
| Redundancy | 3.8 * | 3.5 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 | 293 | 0.2M Na Citrate, 23% PEG 3350, 10% Glycerol, pH 7.5, EVAPORATION, temperature 293K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | Tris | 20 (mM) | pH7.5 |
| 2 | 1 | drop | EDTA | 1 (mM) | |
| 3 | 1 | drop | glycerol | 10 (%) | |
| 4 | 1 | drop | protein | 21.5 (mg/ml) | |
| 5 | 1 | reservoir | sodium citrate | 0.2 (mM) | |
| 6 | 1 | reservoir | PEG4000 | 10 (%) | |
| 7 | 1 | reservoir | glycerol | 5 (%) | |
| 8 | 1 | reservoir | propanol | 10 (%) |
