1UDN
Crystal structure of the tRNA processing enzyme RNase PH from Aquifex aeolicus
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL41XU |
Synchrotron site | SPring-8 |
Beamline | BL41XU |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-03-06 |
Detector | MARRESEARCH |
Wavelength(s) | 1.0 |
Spacegroup name | P 63 2 2 |
Unit cell lengths | 145.441, 145.441, 82.484 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 50.000 * - 2.300 |
R-factor | 0.233 |
Rwork | 0.233 |
R-free | 0.27500 |
Structure solution method | MAD |
RMSD bond length | 0.012 |
RMSD bond angle | 1.600 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.380 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.064 | 0.453 |
Number of reflections | 23052 | |
<I/σ(I)> | 22.1 | 2.1 |
Completeness [%] | 98.8 | 98.9 |
Redundancy | 13 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 * | 20 * | ammonium sulfate, pH 5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | Tris-HCl | 20 (mM) | pH8.0 |
2 | 1 | drop | 5 (mM) | ||
3 | 1 | drop | 50 (mM) | ||
4 | 1 | drop | 10 (mM) | ||
5 | 1 | drop | protein | 1.5 (mg/ml) | |
6 | 1 | reservoir | ammonium sulfate | 2 (M) |