1JL2
Crystal structure of TCEO RNase H-a chimera combining the folding core from T. thermophilus RNase H and the remaining region of E. coli RNase H
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL9-2 |
Synchrotron site | SSRL |
Beamline | BL9-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2000-02-28 |
Detector | MARRESEARCH |
Wavelength(s) | 1.0 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 56.195, 87.033, 60.687 |
Unit cell angles | 90.00, 91.87, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.760 |
R-factor | 0.249 * |
Rwork | 0.249 |
R-free | 0.28590 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1f21 |
RMSD bond length | 0.005 * |
RMSD bond angle | 1.250 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.830 |
High resolution limit [Å] | 1.760 | 1.760 |
Rmerge | 0.061 | 0.277 |
Total number of observations | 62607 * | |
Number of reflections | 5255 * | 189 * |
Completeness [%] | 97.7 | 95.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 298 | 50 mM Tris, pH 8.0, 18% PEG600, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 6 (mg/ml) | |
2 | 1 | reservoir | Tris | 50 (mM) | pH8.0 |
3 | 1 | reservoir | PEG600 | 18 (%) |