1H0O
Cobalt substitution of mouse R2 ribonucleotide reductase to model the reactive diferrous state
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2001-03-15 |
Detector | MARRESEARCH |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 75.900, 106.570, 91.620 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.200 |
R-factor | 0.235 |
Rwork | 0.235 |
R-free | 0.28200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1xsm |
RMSD bond length | 0.010 |
RMSD bond angle | 19.550 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 30.000 |
High resolution limit [Å] | 2.200 |
Number of reflections | 22045 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 4.7 | 0.1 M NA-ACETATE BUFFER PH4.7, 1.2 M NACL, 7.5 MG/ML APO-R2 PROTEIN. CRYSTALS WERE MADE BY CO-CRYSTALLISATION (3.8 EQV. CO2+)., pH 4.70 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 7.5 (mg/ml) | |
2 | 1 | reservoir | sodium acetate | 0.1 (M) | pH4.7 |
3 | 1 | reservoir | 1.2 (M) |