4S0Q
The X-ray structure of the adduct formed in the reaction between bovine pancreatic ribonuclease and carboplatin
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 100 |
Wavelength(s) | 1.5418 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 100.521, 32.499, 72.711 |
Unit cell angles | 90.00, 89.59, 90.00 |
Refinement procedure
Resolution | 72.710 - 2.090 |
R-factor | 0.20801 |
Rwork | 0.205 |
R-free | 0.26175 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | pdb code 1JVT chain A without water molecules and ligands |
RMSD bond length | 0.016 |
RMSD bond angle | 1.762 |
Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 72.710 |
High resolution limit [Å] | 2.090 |
Rmerge | 0.124 |
Number of reflections | 14095 |
Completeness [%] | 99.7 |
Redundancy | 5.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5 | 298 | Crystals of the RNase A-carboplatin adduct have been obtained by soaking experiments where pre-grown monoclinic protein crystals were incubated with an excess of the platinum drug (at a protein to platinum ratio 1:10). Crystals of RNase A were grown by hanging-drop vapor mixing 1 L of RNase A at 20 mg mL-1 with equal volumes of reservoir solution containing 20% PEG4000 and 20 mM sodium citrate buffer pH 5.0 at 298 K. Two weeks after their appearance, crystals were soaked for four days in a solution of Carboplatin dissolved in 10 L of reservoir. At the final, Pt drug:protein concentrations were in 10:1 ratio., VAPOR DIFFUSION, HANGING DROP |