2CVT
Structures of Yeast Ribonucleotide Reductase I
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 14-ID-B |
| Synchrotron site | APS |
| Beamline | 14-ID-B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-11-04 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.82649 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 110.253, 117.071, 63.337 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 3.200 |
| R-factor | 0.22909 |
| Rwork | 0.226 |
| R-free | 0.29792 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | native structure |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.976 |
| 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 | 3.310 |
| High resolution limit [Å] | 3.200 | 3.200 |
| Rmerge | 0.081 | 0.305 |
| Number of reflections | 13023 | |
| <I/σ(I)> | 13 | 5.1 |
| Completeness [%] | 92.1 | 67.8 |
| Redundancy | 9.2 | 7.4 |
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 |
