1GKU
Reverse gyrase from Archaeoglobus fulgidus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Collection date | 2001-02-15 |
| Detector | ADSC |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 65.198, 67.985, 129.728 |
| Unit cell angles | 90.00, 104.01, 90.00 |
Refinement procedure
| Resolution | 41.000 - 2.700 |
| R-factor | 0.226 |
| Rwork | 0.226 |
| R-free | 0.29500 |
| Structure solution method | MAD |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.300 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | SOLVE/RESOLVE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 41.000 | 2.780 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.062 * | 0.288 * |
| Number of reflections | 28735 | |
| <I/σ(I)> | 8.6 | 2.6 |
| Completeness [%] | 99.3 | 99.3 |
| Redundancy | 3.2 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 8 * | 18 * | 15% PEG 1000, 15% ETHYLENE GLYCOL, 100 MM CACODYLATE (PH 6) |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | Tris-HCl | 20 (mM) | pH8.0 |
| 2 | 1 | drop | 200 (mM) | ||
| 3 | 1 | drop | 10 (mM) | ||
| 4 | 1 | drop | EDTA | 1 (mM) | |
| 5 | 1 | drop | 0.02 (%) | ||
| 6 | 1 | drop | protein | 10 (mg/ml) | |
| 7 | 1 | reservoir | PEG1000 | 15 (%) | |
| 8 | 1 | reservoir | ethylene glycol | 15 (%) | |
| 9 | 1 | reservoir | cacodylate | 100 (mM) | pH6. |
