2AV8
Y122F MUTANT OF RIBONUCLEOTIDE REDUCTASE FROM ESCHERICHIA COLI
Experimental procedure
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL7-1 |
Synchrotron site | SSRL |
Beamline | BL7-1 |
Temperature [K] | 103 |
Detector technology | IMAGE PLATE |
Collection date | 1996-08 |
Spacegroup name | P 61 |
Unit cell lengths | 136.500, 136.500, 109.600 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 7.000 - 2.460 |
R-factor | 0.181 |
Rwork | 0.181 |
R-free | 0.23700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1rib |
RMSD bond length | 0.022 |
RMSD bond angle | 21.290 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR (3.8) |
Refinement software | X-PLOR (3.8) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 2.550 |
High resolution limit [Å] | 2.460 | 2.460 |
Rmerge | 0.056 * | |
Number of reflections | 39923 | |
<I/σ(I)> | 14.4 | 2.4 |
Completeness [%] | 95.0 | 83 * |
Redundancy | 2.55 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7.6 | PROTEIN WAS CRYSTALLIZED FROM 80% SATURATED NACL, NEAR PHYSIOLOGICAL PH (PH 7.6) |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | drop | Tris | 50 (mM) | |
3 | 1 | drop | glycerol | 5 (%) | |
4 | 1 | reservoir | 80 (%sat) |