6R1R
RIBONUCLEOTIDE REDUCTASE E441D MUTANT R1 PROTEIN FROM ESCHERICHIA COLI
Experimental procedure
Source type | SYNCHROTRON |
Source details | NSLS |
Synchrotron site | NSLS |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1995-11 |
Detector | RIGAKU |
Spacegroup name | H 3 2 |
Unit cell lengths | 224.490, 224.490, 336.250 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 - 3.100 |
R-factor | 0.202 |
Rwork | 0.194 |
R-free | 0.24000 |
Structure solution method | RIGID BODY |
Starting model (for MR) | 5r1r |
RMSD bond length | 0.009 * |
RMSD bond angle | 2.300 * |
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 | 3.200 |
High resolution limit [Å] | 3.100 | 3.100 |
Rmerge | 0.110 | 0.350 |
Number of reflections | 52995 | |
<I/σ(I)> | 10.8 | 2.5 |
Completeness [%] | 89.7 | 88.9 |
Redundancy | 3 | 2.7 |
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 OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 17 (mg/ml) | |
2 | 1 | reservoir | lithium sulfate | 17 (%) | |
3 | 1 | reservoir | magnesium sulfate | 10 (mM) | |
4 | 1 | reservoir | citrate | 25 (mM) |