1PYL
Crystal structure of Ribonuclease Sa2
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 298 |
Detector technology | IMAGE PLATE |
Collection date | 1997-06-30 |
Detector | RIGAKU |
Wavelength(s) | 1.5418 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 84.980, 34.130, 72.270 |
Unit cell angles | 90.00, 109.50, 90.00 |
Refinement procedure
Resolution | 25.000 - 1.507 |
R-factor | 0.15009 |
Rwork | 0.149 |
R-free | 0.17230 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1rgg |
RMSD bond length | 0.014 |
RMSD bond angle | 1.540 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 1.550 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.063 | 0.272 |
Number of reflections | 30643 | |
<I/σ(I)> | 22.3 | 2.65 |
Completeness [%] | 98.6 | 90.2 |
Redundancy | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.2 | 293 | ammonium sulfate, phosphate buffer, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K |