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 |






