2R1R
RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH DTTP OCCUPYING THE SPECIFICITY SITE FROM ESCHERICHIA COLI
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX9.6 |
| Synchrotron site | SRS |
| Beamline | PX9.6 |
| Temperature [K] | 283 |
| Collection date | 1993-11 |
| 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 - 3.000 |
| R-factor | 0.26 |
| Rwork | 0.238 |
| R-free | 0.28000 |
| Structure solution method | RIGID BODY |
| RMSD bond length | 0.009 * |
| RMSD bond angle | 2.200 * |
| 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 | 3.100 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Rmerge | 0.095 | 0.350 |
| Number of reflections | 68245 | |
| <I/σ(I)> | 12.3 | 3.4 |
| Completeness [%] | 83.0 | 43 |
| Redundancy | 2.6 | 2.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 6 | PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | proteinase | 17 (mg/ml) | |
| 2 | 1 | drop | peptide | 20-fold excess | |
| 3 | 1 | drop | dTTP | 10 (mM) | |
| 4 | 1 | drop | CDP | 10 (mM) | |
| 5 | 1 | reservoir | 17 (%) | ||
| 6 | 1 | reservoir | 10 (mM) | ||
| 7 | 1 | reservoir | citrate | 25 (mM) | pH6.0 |
