1PEO
Ribonucleotide Reductase Protein R1E from Salmonella typhimurium
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 | 2002-07-22 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.9393 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 98.938, 98.938, 289.151 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.000 - 3.000 |
| R-factor | 0.20847 |
| Rwork | 0.206 |
| R-free | 0.25240 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | poly-alanin model of ribonucleotide reductase protein R1 from E.coli |
| RMSD bond length | 0.029 |
| RMSD bond angle | 2.359 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 3.050 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Rmerge | 0.110 | 0.450 |
| Number of reflections | 28924 | |
| <I/σ(I)> | 17.6 | 4.1 |
| Completeness [%] | 99.8 | 98.4 |
| Redundancy | 10.35 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.2 | 288 | sodium malonate, magnesium chloride, DTT, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 288K |
