1PY3
Crystal structure of Ribonuclease Sa2
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X31 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X31 |
Temperature [K] | 293 |
Detector technology | AREA DETECTOR |
Collection date | 1996-04-17 |
Detector | MARRESEARCH |
Wavelength(s) | 0.9185 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 102.290, 68.700, 57.510 |
Unit cell angles | 90.00, 100.40, 90.00 |
Refinement procedure
Resolution | 15.000 - 1.800 |
R-factor | 0.17484 |
Rwork | 0.172 |
R-free | 0.21825 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1rgg |
RMSD bond length | 0.021 |
RMSD bond angle | 1.832 |
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] | 15.000 | 1.830 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.052 | 0.378 |
Number of reflections | 35955 | |
<I/σ(I)> | 20.5 | 2.96 |
Completeness [%] | 99.2 | 98.4 |
Redundancy | 3.45 | 2.8 |
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 |