3O4N
Crystal structure of the Rous Associated Virus Integrase catalytic domain in MES buffer pH 6.0
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-03-07 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.281060 |
Spacegroup name | P 61 |
Unit cell lengths | 107.500, 107.500, 50.920 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 19.680 - 1.800 |
R-factor | 0.19074 |
Rwork | 0.189 |
R-free | 0.22632 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1vsd |
RMSD bond length | 0.029 |
RMSD bond angle | 2.118 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | AMoRE |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.950 |
High resolution limit [Å] | 1.800 | 1.800 |
Number of reflections | 30860 | |
<I/σ(I)> | 11.61 | 3.44 |
Completeness [%] | 99.0 | 100 |
Redundancy | 5.25 | 5.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6 | 290 | 10 mM ZnCl2, 20% (w/v) PEG 6000, 100 mM MES, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 290K |