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) |