1R1R
RIBONUCLEOTIDE REDUCTASE R1 PROTEIN MUTANT Y730F WITH A REDUCED ACTIVE SITE FROM ESCHERICHIA COLI
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X11 |
| Temperature [K] | 278 |
| Detector technology | IMAGE PLATE |
| Collection date | 1995-06 |
| Detector | MARRESEARCH |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 227.820, 227.820, 343.470 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 2.900 |
| R-factor | 0.22 |
| Rwork | 0.210 |
| R-free | 0.24500 |
| Structure solution method | RIGID BODY |
| RMSD bond length | 0.007 * |
| RMSD bond angle | 1.700 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | TNT |
| Refinement software | TNT |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 3.000 |
| High resolution limit [Å] | 2.900 | 2.900 |
| Rmerge | 0.087 | 0.373 * |
| Number of reflections | 77589 | |
| <I/σ(I)> | 15.6 | 2.7 |
| Completeness [%] | 96.0 | 52.2 * |
| Redundancy | 3.3 | 2.3 |
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) | pH6.0 |
| 4 | 1 | drop | protein | 30 (mg/ml) | |
| 5 | 1 | drop | peptide solution | 15 (mg/ml) |
