3HG6
Crystal Structure of the Recombinant Onconase from Rana pipiens
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM16 |
Synchrotron site | ESRF |
Beamline | BM16 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-11-01 |
Detector | MAR CCD 165 mm |
Wavelength(s) | 0.90750 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 32.516, 39.799, 68.536 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 14.700 - 1.700 |
R-factor | 0.187 |
Rwork | 0.185 |
R-free | 0.23700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1onc |
RMSD bond length | 0.015 |
RMSD bond angle | 2.221 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 14.700 | 1.760 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.128 | 0.498 |
Number of reflections | 9807 | |
<I/σ(I)> | 15.403 | 3.84 |
Completeness [%] | 95.5 | 83.6 |
Redundancy | 12.8 | 10.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | capillary contradiffusion | 4 | 288 | 4 M Ammonium sulphate and 0.1 M sodium acetate, capillary contradiffusion, temperature 288K |