3R1R
RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH AMPPNP OCCUPYING THE ACTIVITY SITE FROM ESCHERICHIA COLI
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X12B |
| Synchrotron site | NSLS |
| Beamline | X12B |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1996-07 |
| Detector | MAR scanner 300 mm plate |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 224.610, 224.610, 336.630 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 3.000 |
| R-factor | 0.263 |
| R-free | 0.28700 |
| Structure solution method | RIGID BODY |
| RMSD bond length | 0.015 * |
| RMSD bond angle | 3.000 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | TNT |
| Refinement software | TNT |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 3.110 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Rmerge | 0.121 | 0.350 |
| Number of reflections | 68245 | |
| <I/σ(I)> | 10.1 | 2.4 |
| Completeness [%] | 96.1 * | 42.7 * |
| Redundancy | 4.3 | 2 |
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) |
