1IO2
Crystal structure of type 2 ribonuclease h from hyperthermophilic archaeon, thermococcus kodakaraensis kod1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE BL-6A |
Synchrotron site | Photon Factory |
Beamline | BL-6A |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1999-11-19 |
Detector | FUJI |
Wavelength(s) | 1.0000 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 43.540, 72.990, 78.320 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.000 - 2.000 |
R-factor | 0.223 |
Rwork | 0.223 |
R-free | 0.27400 |
Structure solution method | MIR |
RMSD bond length | 0.005 |
RMSD bond angle | 21.900 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MLPHARE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.054 | 0.254 |
Number of reflections | 15205 | |
<I/σ(I)> | 17.8 | 4.6 |
Completeness [%] | 86.6 | 73.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | PEG 6000, pH 6.50, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG6000 | 15 (%(w/v)) | |
2 | 1 | reservoir | MES | 200 (mM) |