1GL9
Archaeoglobus fulgidus reverse gyrase complexed with ADPNP
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 | 132.410, 68.690, 134.000 |
Unit cell angles | 90.00, 99.70, 90.00 |
Refinement procedure
Resolution | 34.000 - 3.200 |
R-factor | 0.256 |
Rwork | 0.256 |
R-free | 0.33200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1gku |
RMSD bond length | 0.008 |
RMSD bond angle | 1.300 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | CNS (1.1) |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 34.000 | 3.350 |
High resolution limit [Å] | 3.200 | 3.200 |
Rmerge | 0.102 * | 0.321 * |
Number of reflections | 38401 * | |
<I/σ(I)> | 5.2 | 2.3 |
Completeness [%] | 96.7 | 96.7 |
Redundancy | 3.3 | 2.9 |
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),2MM ADPNP |
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 | cacodylate | 100 (mM) | pH6. |