2VBJ
Molecular basis of human XPC gene recognition and cleavage by engineered homing endonuclease heterodimers
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC CCD |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 44.552, 68.700, 88.731 |
Unit cell angles | 90.00, 95.36, 90.00 |
Refinement procedure
Resolution | 32.880 - 1.950 |
R-factor | 0.15 |
Rwork | 0.147 |
R-free | 0.21600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1g9z |
RMSD bond length | 0.014 |
RMSD bond angle | 2.081 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 32.880 | 2.001 |
High resolution limit [Å] | 1.950 | 1.950 |
Rmerge | 0.050 | 0.050 |
Number of reflections | 35740 | |
Completeness [%] | 96.7 | 96.7 |
Redundancy | 4.1 | 4.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | HANGING-DROP DNA-PROTEIN COMPLEX SOLUTION WAS 4 MG/ML. 35% 2-ETHOXYETHANOL IN 0.1M NA-CACODYLATE PH6.5 |