1RNF
X-RAY CRYSTAL STRUCTURE OF UNLIGANDED HUMAN RIBONUCLEASE 4
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 298 |
Detector technology | IMAGE PLATE |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 32.910, 94.270, 40.750 |
Unit cell angles | 90.00, 106.97, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.100 |
R-factor | 0.174 |
Rwork | 0.174 |
R-free | 0.23600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2rat |
RMSD bond length | 0.012 |
RMSD bond angle | 1.601 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.180 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.099 | |
Total number of observations | 57662 * | |
Number of reflections | 13467 * | |
<I/σ(I)> | 8.2 | 2.56 |
Completeness [%] | 97.7 | 94.8 |
Redundancy | 4.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6.9 | 30% PEG4000, 0.1 M SODIUM CADODYLATE, PH 6.3, pH 6.9 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 15 (mg/ml) | |
2 | 1 | reservoir | PEG4000 | 15 (%(v/v)) | |
3 | 1 | reservoir | sodium acetate | 0.1 (M) |