3P56
The structure of the human RNase H2 complex defines key interaction interfaces relevant to enzyme function and human disease
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I04 |
Synchrotron site | Diamond |
Beamline | I04 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-08-09 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9793 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 212.238, 42.302, 186.950 |
Unit cell angles | 90.00, 98.11, 90.00 |
Refinement procedure
Resolution | 30.000 - 4.060 |
R-factor | 0.3747 |
Rwork | 0.374 |
R-free | 0.37900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | re-refined PDB ID: 3KIO |
RMSD bond length | 0.008 |
RMSD bond angle | 0.960 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | BUSTER-TNT |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 30.000 | 30.000 | 4.250 |
High resolution limit [Å] | 4.060 | 8.770 | 4.060 |
Rmerge | 0.180 | 0.076 | 0.690 |
Number of reflections | 13282 | ||
<I/σ(I)> | 3.6 | ||
Completeness [%] | 98.5 | 97.4 | 98.7 |
Redundancy | 3.9 | 4.1 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 277.15 | 20% PEG 3350, 0.1M bis-Tris pH6.5, 0.2M KNO3, vapor diffusion, sitting drop, temperature 277.15K |