1Q8R
Structure of E.coli RusA Holliday junction resolvase
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2001-04-25 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.97943 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 45.352, 50.052, 49.597 |
Unit cell angles | 90.00, 101.42, 90.00 |
Refinement procedure
Resolution | 19.200 * - 1.900* |
R-factor | 0.19199 |
Rwork | 0.190 |
R-free | 0.22600 * |
Structure solution method | MAD |
Starting model (for MR) | NONE |
RMSD bond length | 0.014 * |
RMSD bond angle | 2.800 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SHELXD |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.950 |
High resolution limit [Å] | 1.900 * | 1.900 * |
Rmerge | 0.028 | 0.103 |
Number of reflections | 17267 | |
<I/σ(I)> | 12.25 | 8.58 |
Completeness [%] | 99.0 * | 97 |
Redundancy | 3.7 | 3.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 290 | PEG 4000, sodium acetate, Tris-HCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 290K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 5 (mg/ml) | |
2 | 1 | reservoir | PEG4000 | 30 (%) | |
3 | 1 | reservoir | sodium acetate | 0.3 (M) | in Tris-HCl, pH8 |