2CVX
Structures of Yeast Ribonucleotide Reductase I
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 14-BM-C |
| Synchrotron site | APS |
| Beamline | 14-BM-C |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-03-12 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.90000 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 107.687, 117.277, 65.061 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.200 |
| R-factor | 0.21462 |
| Rwork | 0.210 |
| R-free | 0.25428 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | native structure |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.454 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | REFMAC (5.2.0007) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.280 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.063 | 0.123 |
| Number of reflections | 42470 | |
| <I/σ(I)> | 12.3 | 6.3 |
| Completeness [%] | 99.1 | 97 |
| Redundancy | 6.1 | 5.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 6.5 | 298 | PEG 3350, sodium acetate, ammonium sulfate, pH 6.5, EVAPORATION, temperature 298K |
