1RLR
STRUCTURE OF RIBONUCLEOTIDE REDUCTASE PROTEIN R1
Experimental procedure
| Spacegroup name | H 3 2 |
| Unit cell lengths | 226.000, 226.000, 341.000 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 7.000 - 2.500 |
| R-factor | 0.21 |
| Rwork | 0.210 |
| RMSD bond length | 0.019 |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 2.500 * |
| Rmerge | 0.098 * |
| Number of reflections | 109500 |
| Completeness [%] | 94.0 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 6 * | Uhlin, U., (1993) FEBS Lett., 336, 148. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | lithium sulphate | 17 (%) | |
| 2 | 1 | reservoir | magnesium sulphate | 10 (mM) | |
| 3 | 1 | reservoir | sodium citrate | 25 (mM) | |
| 4 | 1 | drop | protein | 15 (mg/ml) | |
| 5 | 1 | drop | lithium sulphate | 8.5 (%) | |
| 6 | 1 | drop | magnesium sulphate | 5 (mM) | |
| 7 | 1 | drop | sodium citrate | 12.5 (mM) |
