1MXR
High resolution structure of Ribonucleotide reductase R2 from E. coli in its oxidised (Met) form
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM1A |
Synchrotron site | ESRF |
Beamline | BM1A |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1999-02-08 |
Detector | MARRESEARCH |
Wavelength(s) | 0.87961 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 73.844, 84.975, 114.318 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.000 * - 1.420 |
R-factor | 0.16 |
Rwork | 0.160 |
R-free | 0.18500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | reduced e. coli RNR R2 (1XIK) |
RMSD bond length | 0.013 |
RMSD bond angle | 1.510 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 1.470 |
High resolution limit [Å] | 1.420 | 1.420 |
Rmerge | 0.064 * | 0.288 |
Total number of observations | 603231 * | |
Number of reflections | 123371 | |
Completeness [%] | 90.8 | 91.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 20 * | Nordlund, P. (1989) FEBS Lett., 258, 251. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG4000 | 20 (%) | |
2 | 1 | reservoir | 0.2 (M) | ||
3 | 1 | reservoir | dioxane | 3 (%) | |
4 | 1 | reservoir | MES | 0.05 (M) | |
5 | 1 | reservoir | EMTS |